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overflow: hidden; text-overflow: ellipsis; -webkit-line-clamp: 3; -webkit-box-orient: vertical; }</style><div class="col-xs-12 clearfix"><div class="u-floatLeft"><h1 class="PageHeader-title u-m0x u-fs30">Biophysical Chemistry</h1><div class="u-tcGrayDark">10,023 Followers</div><div class="u-tcGrayDark u-mt2x">Recent papers in <b>Biophysical Chemistry</b></div></div></div></div></div></div><div class="TabbedNavigation"><div class="container"><div class="row"><div class="col-xs-12 clearfix"><ul class="nav u-m0x u-p0x list-inline u-displayFlex"><li class="active"><a href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Top Papers</a></li><li><a href="https://www.academia.edu/Documents/in/Biophysical_Chemistry/MostCited">Most Cited Papers</a></li><li><a href="https://www.academia.edu/Documents/in/Biophysical_Chemistry/MostDownloaded">Most Downloaded Papers</a></li><li><a href="https://www.academia.edu/Documents/in/Biophysical_Chemistry/MostRecent">Newest Papers</a></li><li><a class="" href="https://www.academia.edu/People/Biophysical_Chemistry">People</a></li></ul></div><style type="text/css">ul.nav{flex-direction:row}@media(max-width: 567px){ul.nav{flex-direction:column}.TabbedNavigation li{max-width:100%}.TabbedNavigation li.active{background-color:var(--background-grey, #dddde2)}.TabbedNavigation li.active:before,.TabbedNavigation li.active:after{display:none}}</style></div></div></div><div class="container"><div class="row"><div class="col-xs-12"><div class="u-displayFlex"><div class="u-flexGrow1"><div class="works"><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_47104073" data-work_id="47104073" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/47104073/Water_and_Backbone_Dynamics_in_a_Hydrated_Protein">Water and Backbone Dynamics in a Hydrated Protein</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Rotational immobilization of proteins permits characterization of the internal peptide and water molecule dynamics by magnetic relaxation dispersion spectroscopy. Using different experimental approaches, we have extended measurements of... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_47104073" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Rotational immobilization of proteins permits characterization of the internal peptide and water molecule dynamics by magnetic relaxation dispersion spectroscopy. Using different experimental approaches, we have extended measurements of the magnetic field dependence of the proton-spin-lattice-relaxation rate by one decade from 0.01 to 300 MHz for 1 H and showed that the underlying dynamics driving the protein 1 H spin-lattice relaxation is preserved over 4.5 decades in frequency. This extension is critical to understanding the role of 1 H 2 O in the total proton-spin-relaxation process. The fact that the proteinproton-relaxation-dispersion profile is a power law in frequency with constant coefficient and exponent over nearly 5 decades indicates that the characteristics of the native protein structural fluctuations that cause proton nuclear spin-lattice relaxation are remarkably constant over this wide frequency and length-scale interval. Comparison of protein-proton-spin-lattice-relaxation rate constants in protein gels equilibrated with 2 H 2 O rather than 1 H 2 O shows that water protons make an important contribution to the total spin-lattice relaxation in the middle of this frequency range for hydrated proteins because of water molecule dynamics in the time range of tens of ns. This water contribution is with the motion of relatively rare, long-lived, and perhaps buried water molecules constrained by the confinement. The presence of water molecule reorientational dynamics in the tens of ns range that are sufficient to affect the spin-lattice relaxation driven by 1 H dipole-dipole fluctuations should make the local dielectric properties in the protein frequency dependent in a regime relevant to catalytically important kinetic barriers to conformational rearrangements.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/47104073" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="806dad1e1e16dbfbf9101e948d055c95" rel="nofollow" data-download="{"attachment_id":66374754,"asset_id":47104073,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/66374754/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="39593482" href="https://virginia.academia.edu/GalinaDiakova">Galina Diakova</a><script data-card-contents-for-user="39593482" type="text/json">{"id":39593482,"first_name":"Galina","last_name":"Diakova","domain_name":"virginia","page_name":"GalinaDiakova","display_name":"Galina Diakova","profile_url":"https://virginia.academia.edu/GalinaDiakova?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_47104073 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="47104073"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 47104073, container: ".js-paper-rank-work_47104073", }); 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Using different experimental approaches, we have extended measurements of the magnetic field dependence of the proton-spin-lattice-relaxation rate by one decade from 0.01 to 300 MHz for 1 H and showed that the underlying dynamics driving the protein 1 H spin-lattice relaxation is preserved over 4.5 decades in frequency. This extension is critical to understanding the role of 1 H 2 O in the total proton-spin-relaxation process. The fact that the proteinproton-relaxation-dispersion profile is a power law in frequency with constant coefficient and exponent over nearly 5 decades indicates that the characteristics of the native protein structural fluctuations that cause proton nuclear spin-lattice relaxation are remarkably constant over this wide frequency and length-scale interval. Comparison of protein-proton-spin-lattice-relaxation rate constants in protein gels equilibrated with 2 H 2 O rather than 1 H 2 O shows that water protons make an important contribution to the total spin-lattice relaxation in the middle of this frequency range for hydrated proteins because of water molecule dynamics in the time range of tens of ns. This water contribution is with the motion of relatively rare, long-lived, and perhaps buried water molecules constrained by the confinement. The presence of water molecule reorientational dynamics in the tens of ns range that are sufficient to affect the spin-lattice relaxation driven by 1 H dipole-dipole fluctuations should make the local dielectric properties in the protein frequency dependent in a regime relevant to catalytically important kinetic barriers to conformational rearrangements.","downloadable_attachments":[{"id":66374754,"asset_id":47104073,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":39593482,"first_name":"Galina","last_name":"Diakova","domain_name":"virginia","page_name":"GalinaDiakova","display_name":"Galina Diakova","profile_url":"https://virginia.academia.edu/GalinaDiakova?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2215,"name":"Water","url":"https://www.academia.edu/Documents/in/Water?f_ri=19156","nofollow":true},{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":34754,"name":"Magnetic field","url":"https://www.academia.edu/Documents/in/Magnetic_field?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":69542,"name":"Computer Simulation","url":"https://www.academia.edu/Documents/in/Computer_Simulation?f_ri=19156"},{"id":113890,"name":"Power Law","url":"https://www.academia.edu/Documents/in/Power_Law?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":166367,"name":"Protein structure","url":"https://www.academia.edu/Documents/in/Protein_structure?f_ri=19156"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=19156"},{"id":186260,"name":"Dielectric Properties","url":"https://www.academia.edu/Documents/in/Dielectric_Properties?f_ri=19156"},{"id":190381,"name":"Spin Relaxation","url":"https://www.academia.edu/Documents/in/Spin_Relaxation?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":349439,"name":"Frequency Dependence","url":"https://www.academia.edu/Documents/in/Frequency_Dependence?f_ri=19156"},{"id":414692,"name":"Solutions","url":"https://www.academia.edu/Documents/in/Solutions?f_ri=19156"},{"id":453823,"name":"Length scale","url":"https://www.academia.edu/Documents/in/Length_scale?f_ri=19156"},{"id":945575,"name":"Electric Dipole Moments","url":"https://www.academia.edu/Documents/in/Electric_Dipole_Moments?f_ri=19156"},{"id":3430039,"name":"Rate Constant","url":"https://www.academia.edu/Documents/in/Rate_Constant?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_75759394" data-work_id="75759394" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/75759394/The_action_of_local_anesthetics_on_myelin_structure_and_nerve_conduction_in_toad_sciatic_nerve">The action of local anesthetics on myelin structure and nerve conduction in toad sciatic nerve</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">X-ray scattering and electrophysiological experiments were performed on toad sciatic nerves in the presence of local anesthetics. In vitro experiments were performed on dissected nerves superfused with Ringer's solutions containing... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_75759394" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">X-ray scattering and electrophysiological experiments were performed on toad sciatic nerves in the presence of local anesthetics. In vitro experiments were performed on dissected nerves superfused with Ringer's solutions containing procaine, lidocaine, tetracaine, or dibucaine. In vivo experiments were performed on nerves dissected from animals anesthesized by targeted injections of tetracaine-containing solutions. In all cases the anesthetics were found to have the same effects on the x-ray scattering spectra: the intensity ratio of the even-order to the odd-order reflections increases and the lattice parameter increases. These changes are reversible upon removal of the anesthetic. The magnitude of the structural changes varies with the duration of the superfusion and with the nature and concentration of the anesthetic molecule. A striking quantitative correlation was observed between the structural effects and the potency of the anesthetic. Electron density profiles, which hardly showed any structural alteration of the unit membrane, clearly indicated that the anesthetics have the effect of moving the pairs of membranes apart by increasing the thickness of the cytoplasmic space. Electrophysiological measurements performed on the very samples used in the x-ray scattering experiments showed that the amplitude of the compound action potential is affected earlier than the structure of myelin (as revealed by the x-ray scattering experiments), whereas conduction velocity closely follows the structural alterations.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/75759394" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3807b93c5017f06c2a172344e272e021" rel="nofollow" data-download="{"attachment_id":83493457,"asset_id":75759394,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/83493457/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="176842861" href="https://independent.academia.edu/GustavoMarquez48">Gustavo Marquez</a><script data-card-contents-for-user="176842861" type="text/json">{"id":176842861,"first_name":"Gustavo","last_name":"Marquez","domain_name":"independent","page_name":"GustavoMarquez48","display_name":"Gustavo Marquez","profile_url":"https://independent.academia.edu/GustavoMarquez48?f_ri=19156","photo":"https://0.academia-photos.com/176842861/168073255/158032362/s65_gustavo.marquez.png"}</script></span></span></li><li class="js-paper-rank-work_75759394 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="75759394"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 75759394, container: ".js-paper-rank-work_75759394", }); 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In vitro experiments were performed on dissected nerves superfused with Ringer's solutions containing procaine, lidocaine, tetracaine, or dibucaine. In vivo experiments were performed on nerves dissected from animals anesthesized by targeted injections of tetracaine-containing solutions. In all cases the anesthetics were found to have the same effects on the x-ray scattering spectra: the intensity ratio of the even-order to the odd-order reflections increases and the lattice parameter increases. These changes are reversible upon removal of the anesthetic. The magnitude of the structural changes varies with the duration of the superfusion and with the nature and concentration of the anesthetic molecule. A striking quantitative correlation was observed between the structural effects and the potency of the anesthetic. Electron density profiles, which hardly showed any structural alteration of the unit membrane, clearly indicated that the anesthetics have the effect of moving the pairs of membranes apart by increasing the thickness of the cytoplasmic space. Electrophysiological measurements performed on the very samples used in the x-ray scattering experiments showed that the amplitude of the compound action potential is affected earlier than the structure of myelin (as revealed by the x-ray scattering experiments), whereas conduction velocity closely follows the structural alterations.","downloadable_attachments":[{"id":83493457,"asset_id":75759394,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":176842861,"first_name":"Gustavo","last_name":"Marquez","domain_name":"independent","page_name":"GustavoMarquez48","display_name":"Gustavo Marquez","profile_url":"https://independent.academia.edu/GustavoMarquez48?f_ri=19156","photo":"https://0.academia-photos.com/176842861/168073255/158032362/s65_gustavo.marquez.png"}],"research_interests":[{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical 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Sheath","url":"https://www.academia.edu/Documents/in/Myelin_Sheath?f_ri=19156"},{"id":3881526,"name":"In Vitro Techniques","url":"https://www.academia.edu/Documents/in/In_Vitro_Techniques?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_59486178" data-work_id="59486178" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/59486178/Assembly_of_the_Prothrombinase_Complex">Assembly of the Prothrombinase Complex</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/59486178" 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class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33032760" href="https://vermont.academia.edu/PaulaTracy">Paula Tracy</a><script data-card-contents-for-user="33032760" type="text/json">{"id":33032760,"first_name":"Paula","last_name":"Tracy","domain_name":"vermont","page_name":"PaulaTracy","display_name":"Paula Tracy","profile_url":"https://vermont.academia.edu/PaulaTracy?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_59486178 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="59486178"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 59486178, container: ".js-paper-rank-work_59486178", }); });</script></li><li class="js-percentile-work_59486178 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 59486178; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_59486178"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_59486178 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="59486178"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 59486178; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=59486178]").text(description); $(".js-view-count-work_59486178").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_59486178").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="59486178"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">4</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a>, <script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="260118" rel="nofollow" href="https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES">CHEMICAL SCIENCES</a><script data-card-contents-for-ri="260118" type="text/json">{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=59486178]'), work: {"id":59486178,"title":"Assembly of the Prothrombinase Complex","created_at":"2021-10-22T04:37:28.214-07:00","url":"https://www.academia.edu/59486178/Assembly_of_the_Prothrombinase_Complex?f_ri=19156","dom_id":"work_59486178","summary":null,"downloadable_attachments":[{"id":73384768,"asset_id":59486178,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33032760,"first_name":"Paula","last_name":"Tracy","domain_name":"vermont","page_name":"PaulaTracy","display_name":"Paula Tracy","profile_url":"https://vermont.academia.edu/PaulaTracy?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_54131140" data-work_id="54131140" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/54131140/Dissociation_of_Limulus_polyphemus_horseshoe_crab_hemocyanin">Dissociation of Limulus polyphemus (horseshoe crab) hemocyanin</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">A solution X-ray scattering study has been performed on Limulus polyphemus (horseshoe crab) hemocyanin and its dissociated fragments at various pH values in the presence and absence of Ca *'. The scattering patterns of native hemocyanin... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_54131140" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">A solution X-ray scattering study has been performed on Limulus polyphemus (horseshoe crab) hemocyanin and its dissociated fragments at various pH values in the presence and absence of Ca *'. The scattering patterns of native hemocyanin (4%mer), the half molecule (24mer), quarter molecule (Ibmer) and monomer fraction were measured. The radii of gyration for the four molecular species were calculated from the Guinier plots to be 110.7, 91.3, 77.3, and 36.5 A, respectively. Models which yield good fits to the experimental data are presented. The models were constructed using eight, four and two spheres with a radius of 58 A, assuming the sphere to be the submultiple composed of six subunits. The radir of gyration were calculated on the basis of the model and the values found to be 106, 94 and 73 A, respectively, in good agreement with the experimental results.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/54131140" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="1968afda5f6b3262d9f0730a0f43ef8a" rel="nofollow" data-download="{"attachment_id":70644504,"asset_id":54131140,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/70644504/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="53217206" href="https://independent.academia.edu/HiroshiKihara">Hiroshi Kihara</a><script data-card-contents-for-user="53217206" type="text/json">{"id":53217206,"first_name":"Hiroshi","last_name":"Kihara","domain_name":"independent","page_name":"HiroshiKihara","display_name":"Hiroshi Kihara","profile_url":"https://independent.academia.edu/HiroshiKihara?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_54131140 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="54131140"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 54131140, container: ".js-paper-rank-work_54131140", }); });</script></li><li class="js-percentile-work_54131140 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 54131140; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_54131140"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_54131140 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="54131140"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 54131140; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=54131140]").text(description); $(".js-view-count-work_54131140").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_54131140").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="54131140"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">10</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="10636" rel="nofollow" href="https://www.academia.edu/Documents/in/Small_Angle_X_Ray_Scattering">Small Angle X Ray Scattering</a>, <script data-card-contents-for-ri="10636" type="text/json">{"id":10636,"name":"Small Angle X Ray Scattering","url":"https://www.academia.edu/Documents/in/Small_Angle_X_Ray_Scattering?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a><script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=54131140]'), work: {"id":54131140,"title":"Dissociation of Limulus polyphemus (horseshoe crab) hemocyanin","created_at":"2021-09-29T22:11:30.984-07:00","url":"https://www.academia.edu/54131140/Dissociation_of_Limulus_polyphemus_horseshoe_crab_hemocyanin?f_ri=19156","dom_id":"work_54131140","summary":"A solution X-ray scattering study has been performed on Limulus polyphemus (horseshoe crab) hemocyanin and its dissociated fragments at various pH values in the presence and absence of Ca *'. The scattering patterns of native hemocyanin (4%mer), the half molecule (24mer), quarter molecule (Ibmer) and monomer fraction were measured. The radii of gyration for the four molecular species were calculated from the Guinier plots to be 110.7, 91.3, 77.3, and 36.5 A, respectively. Models which yield good fits to the experimental data are presented. The models were constructed using eight, four and two spheres with a radius of 58 A, assuming the sphere to be the submultiple composed of six subunits. The radir of gyration were calculated on the basis of the model and the values found to be 106, 94 and 73 A, respectively, in good agreement with the experimental results.","downloadable_attachments":[{"id":70644504,"asset_id":54131140,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":53217206,"first_name":"Hiroshi","last_name":"Kihara","domain_name":"independent","page_name":"HiroshiKihara","display_name":"Hiroshi Kihara","profile_url":"https://independent.academia.edu/HiroshiKihara?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=19156","nofollow":true},{"id":10636,"name":"Small Angle X Ray Scattering","url":"https://www.academia.edu/Documents/in/Small_Angle_X_Ray_Scattering?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":51757,"name":"Dissociation","url":"https://www.academia.edu/Documents/in/Dissociation?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":463300,"name":"Molecular Model","url":"https://www.academia.edu/Documents/in/Molecular_Model?f_ri=19156"},{"id":664552,"name":"Radius of Gyration","url":"https://www.academia.edu/Documents/in/Radius_of_Gyration?f_ri=19156"},{"id":1354264,"name":"Subunit","url":"https://www.academia.edu/Documents/in/Subunit?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_3498626" data-work_id="3498626" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/3498626/Building_Up_of_the_Liquid_Ordered_Phase_Formed_by_Sphingomyelin_and_Cholesterol">Building Up of the Liquid-Ordered Phase Formed by Sphingomyelin and Cholesterol</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The long-range and molecular orders and dynamics in codispersions of egg sphingomyelin-cholesterol have been investigated by synchrotron x-ray diffraction and electron spin resonance using phosphatidylcholine spin-labeled at several... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_3498626" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The long-range and molecular orders and dynamics in codispersions of egg sphingomyelin-cholesterol have been investigated by synchrotron x-ray diffraction and electron spin resonance using phosphatidylcholine spin-labeled at several positions on the sn-2 chain. Mixtures containing 0, 17, 33, 41, 50 mol% cholesterol exhibited a single phase by x-ray diffraction methods. The temperature dependence of the d-spacing between 20 and 50°C is attenuated with increasing proportions of cholesterol, becoming invariant for cholesterol contents of 41 and 50 mol% on completion of the liquid-ordered phase. Electron spin resonance revealed two sites for 17 and 33 mol% cholesterol. One site is highly ordered and the other is less ordered than the fluid phase of pure sphingomyelin as shown by the molecular and the intramolecular order parameters reflecting the segmental motions of the probe. The two-sites exchange rate indicates a mean lifetime of the sites of ;0.1 ms during which the lipid displacement is ;1 nm. The short lifetime of the sites probed by ESR and the single phase detected by x-ray diffraction support in this binary mixture, the building up of the Lo phase by a progressive accumulation of randomly distributed sphingomyelin-cholesterol condensed complexes rather than by diffusional exchange between extended domains.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/3498626" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="7bc3bfd68d35bd4807f5da300973cddd" rel="nofollow" data-download="{"attachment_id":50261856,"asset_id":3498626,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/50261856/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="4111791" href="https://tbilisi-art.academia.edu/MariKhelashvili">Mari Khelashvili</a><script data-card-contents-for-user="4111791" type="text/json">{"id":4111791,"first_name":"Mari","last_name":"Khelashvili","domain_name":"tbilisi-art","page_name":"MariKhelashvili","display_name":"Mari Khelashvili","profile_url":"https://tbilisi-art.academia.edu/MariKhelashvili?f_ri=19156","photo":"https://0.academia-photos.com/4111791/1589803/1922956/s65_mari.khelashvili.jpg"}</script></span></span></li><li class="js-paper-rank-work_3498626 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="3498626"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 3498626, container: ".js-paper-rank-work_3498626", }); 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$(".js-view-count[data-work-id=3498626]").text(description); $(".js-view-count-work_3498626").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_3498626").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="3498626"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">13</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="502" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysics">Biophysics</a>, <script data-card-contents-for-ri="502" type="text/json">{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="7331" rel="nofollow" href="https://www.academia.edu/Documents/in/Electron_Spin_Resonance">Electron Spin Resonance</a>, <script data-card-contents-for-ri="7331" type="text/json">{"id":7331,"name":"Electron Spin Resonance","url":"https://www.academia.edu/Documents/in/Electron_Spin_Resonance?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a><script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=3498626]'), work: {"id":3498626,"title":"Building Up of the Liquid-Ordered Phase Formed by Sphingomyelin and Cholesterol","created_at":"2013-05-09T02:03:39.715-07:00","url":"https://www.academia.edu/3498626/Building_Up_of_the_Liquid_Ordered_Phase_Formed_by_Sphingomyelin_and_Cholesterol?f_ri=19156","dom_id":"work_3498626","summary":"The long-range and molecular orders and dynamics in codispersions of egg sphingomyelin-cholesterol have been investigated by synchrotron x-ray diffraction and electron spin resonance using phosphatidylcholine spin-labeled at several positions on the sn-2 chain. Mixtures containing 0, 17, 33, 41, 50 mol% cholesterol exhibited a single phase by x-ray diffraction methods. The temperature dependence of the d-spacing between 20 and 50°C is attenuated with increasing proportions of cholesterol, becoming invariant for cholesterol contents of 41 and 50 mol% on completion of the liquid-ordered phase. Electron spin resonance revealed two sites for 17 and 33 mol% cholesterol. One site is highly ordered and the other is less ordered than the fluid phase of pure sphingomyelin as shown by the molecular and the intramolecular order parameters reflecting the segmental motions of the probe. The two-sites exchange rate indicates a mean lifetime of the sites of ;0.1 ms during which the lipid displacement is ;1 nm. The short lifetime of the sites probed by ESR and the single phase detected by x-ray diffraction support in this binary mixture, the building up of the Lo phase by a progressive accumulation of randomly distributed sphingomyelin-cholesterol condensed complexes rather than by diffusional exchange between extended domains.","downloadable_attachments":[{"id":50261856,"asset_id":3498626,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":4111791,"first_name":"Mari","last_name":"Khelashvili","domain_name":"tbilisi-art","page_name":"MariKhelashvili","display_name":"Mari Khelashvili","profile_url":"https://tbilisi-art.academia.edu/MariKhelashvili?f_ri=19156","photo":"https://0.academia-photos.com/4111791/1589803/1922956/s65_mari.khelashvili.jpg"}],"research_interests":[{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true},{"id":7331,"name":"Electron Spin Resonance","url":"https://www.academia.edu/Documents/in/Electron_Spin_Resonance?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":90514,"name":"Cholesterol","url":"https://www.academia.edu/Documents/in/Cholesterol?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":148995,"name":"Long Range","url":"https://www.academia.edu/Documents/in/Long_Range?f_ri=19156"},{"id":154672,"name":"Membrane Lipids","url":"https://www.academia.edu/Documents/in/Membrane_Lipids?f_ri=19156"},{"id":228986,"name":"Exchange rate","url":"https://www.academia.edu/Documents/in/Exchange_rate?f_ri=19156"},{"id":247487,"name":"Temperature Dependence","url":"https://www.academia.edu/Documents/in/Temperature_Dependence?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":386527,"name":"X ray diffraction","url":"https://www.academia.edu/Documents/in/X_ray_diffraction?f_ri=19156"},{"id":960474,"name":"Order Parameter","url":"https://www.academia.edu/Documents/in/Order_Parameter?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_4839235" data-work_id="4839235" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/4839235/High_resolution_scanning_tunneling_microscopy_investigation_of_the_12110_and_10000_two_fold_symmetric_d_AlNiCo_quasicrystalline_surfaces">High-resolution scanning tunneling microscopy investigation of the (12110) and (10000) two-fold symmetric d AlNiCo quasicrystalline surfaces</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Gold nanoparticles protected by a binary mixture of thiolate molecules have a ligand shell that can spontaneously separate into nanoscale domains. Complex morphologies arise in such ligand shells, including striped, patchy, and Janus... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_4839235" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Gold nanoparticles protected by a binary mixture of thiolate molecules have a ligand shell that can spontaneously separate into nanoscale domains. Complex morphologies arise in such ligand shells, including striped, patchy, and Janus domains. Characterization of these morphologies remains a challenge. Scanning tunneling microscopy (STM) imaging has been one of the key approaches to determine these structures, yet the imaging of nanoparticles' surfaces faces difficulty stemming from steep surface curvature, complex molecular structures, and the possibility of imaging artifacts in the same size range. Images obtained to date have lacked molecular resolution, and only domains have been resolved. There is a clear need for images that resolve the molecular arrangement that leads to domain formation on the ligand shell of these particles. Herein we report an advance in the STM imaging of gold nanoparticles, revealing some of the molecules that constitute the domains in striped and Janus gold nanoparticles. We analyze the images to determine molecular arrangements on parts of the particles, highlight molecular "defects" present in the ligand shell, show persistence of the features across subsequent images, and observe the transition from quasimolecular to domain resolution. The ability to resolve single molecules in the ligand shell of nanoparticles could lead to a more comprehensive understanding of the role of the ligand structure in determining the properties of mixed-monolayer-protected gold nanoparticles.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/4839235" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="0fa808cf1c45c57c0711c1d5c4a02d5e" rel="nofollow" data-download="{"attachment_id":49607174,"asset_id":4839235,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/49607174/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="6271074" href="https://independent.academia.edu/SofiaDeloudi">Sofia Deloudi</a><script data-card-contents-for-user="6271074" type="text/json">{"id":6271074,"first_name":"Sofia","last_name":"Deloudi","domain_name":"independent","page_name":"SofiaDeloudi","display_name":"Sofia Deloudi","profile_url":"https://independent.academia.edu/SofiaDeloudi?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_4839235 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="4839235"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 4839235, container: ".js-paper-rank-work_4839235", }); 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Complex morphologies arise in such ligand shells, including striped, patchy, and Janus domains. Characterization of these morphologies remains a challenge. Scanning tunneling microscopy (STM) imaging has been one of the key approaches to determine these structures, yet the imaging of nanoparticles' surfaces faces difficulty stemming from steep surface curvature, complex molecular structures, and the possibility of imaging artifacts in the same size range. Images obtained to date have lacked molecular resolution, and only domains have been resolved. There is a clear need for images that resolve the molecular arrangement that leads to domain formation on the ligand shell of these particles. Herein we report an advance in the STM imaging of gold nanoparticles, revealing some of the molecules that constitute the domains in striped and Janus gold nanoparticles. We analyze the images to determine molecular arrangements on parts of the particles, highlight molecular \"defects\" present in the ligand shell, show persistence of the features across subsequent images, and observe the transition from quasimolecular to domain resolution. The ability to resolve single molecules in the ligand shell of nanoparticles could lead to a more comprehensive understanding of the role of the ligand structure in determining the properties of mixed-monolayer-protected gold nanoparticles.","downloadable_attachments":[{"id":49607174,"asset_id":4839235,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":6271074,"first_name":"Sofia","last_name":"Deloudi","domain_name":"independent","page_name":"SofiaDeloudi","display_name":"Sofia Deloudi","profile_url":"https://independent.academia.edu/SofiaDeloudi?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":48,"name":"Engineering","url":"https://www.academia.edu/Documents/in/Engineering?f_ri=19156","nofollow":true},{"id":56,"name":"Materials Engineering","url":"https://www.academia.edu/Documents/in/Materials_Engineering?f_ri=19156","nofollow":true},{"id":505,"name":"Condensed Matter Physics","url":"https://www.academia.edu/Documents/in/Condensed_Matter_Physics?f_ri=19156","nofollow":true},{"id":518,"name":"Quantum Physics","url":"https://www.academia.edu/Documents/in/Quantum_Physics?f_ri=19156","nofollow":true},{"id":923,"name":"Technology","url":"https://www.academia.edu/Documents/in/Technology?f_ri=19156"},{"id":2215,"name":"Water","url":"https://www.academia.edu/Documents/in/Water?f_ri=19156"},{"id":2465,"name":"Surface Science","url":"https://www.academia.edu/Documents/in/Surface_Science?f_ri=19156"},{"id":17733,"name":"Nanotechnology","url":"https://www.academia.edu/Documents/in/Nanotechnology?f_ri=19156"},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary?f_ri=19156"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":50105,"name":"Scanning tunneling microscopy","url":"https://www.academia.edu/Documents/in/Scanning_tunneling_microscopy?f_ri=19156"},{"id":52770,"name":"Molecular Electronics","url":"https://www.academia.edu/Documents/in/Molecular_Electronics?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":133177,"name":"Temperature","url":"https://www.academia.edu/Documents/in/Temperature?f_ri=19156"},{"id":158165,"name":"Zinc","url":"https://www.academia.edu/Documents/in/Zinc?f_ri=19156"},{"id":217265,"name":"Ultramicroscopy","url":"https://www.academia.edu/Documents/in/Ultramicroscopy?f_ri=19156"},{"id":219635,"name":"Electronic Structure","url":"https://www.academia.edu/Documents/in/Electronic_Structure?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":263152,"name":"Optical physics","url":"https://www.academia.edu/Documents/in/Optical_physics?f_ri=19156"},{"id":309086,"name":"High Resolution","url":"https://www.academia.edu/Documents/in/High_Resolution?f_ri=19156"},{"id":317484,"name":"Fine Structure Constant","url":"https://www.academia.edu/Documents/in/Fine_Structure_Constant?f_ri=19156"},{"id":319122,"name":"Surface Structure","url":"https://www.academia.edu/Documents/in/Surface_Structure?f_ri=19156"},{"id":480226,"name":"Surface Charge","url":"https://www.academia.edu/Documents/in/Surface_Charge?f_ri=19156"},{"id":616972,"name":"Low Temperature","url":"https://www.academia.edu/Documents/in/Low_Temperature?f_ri=19156"},{"id":758900,"name":"Lipid bilayers","url":"https://www.academia.edu/Documents/in/Lipid_bilayers?f_ri=19156"},{"id":1029221,"name":"Freezing","url":"https://www.academia.edu/Documents/in/Freezing?f_ri=19156"},{"id":1261153,"name":"Atomic Resolution","url":"https://www.academia.edu/Documents/in/Atomic_Resolution?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_65928060" data-work_id="65928060" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/65928060/Isolation_and_characterization_of_5_lipoxygenase_from_tulip_bulbs">Isolation and characterization of 5-lipoxygenase from tulip bulbs</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Lipoxygenases are a group of closely related enzymes responsible for the dioxygenation of various polyenoic fatty acids containing all-cis-methylene-interrupted double bonds. The nomenclature for lipoxygenases is based on the site of... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_65928060" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Lipoxygenases are a group of closely related enzymes responsible for the dioxygenation of various polyenoic fatty acids containing all-cis-methylene-interrupted double bonds. 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Biophysical Society National Lecture, 1992</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Looking at proteins is an active process of interpretation and selection, emphasizing some features and deleting others. Multiple representations are needed, for such purposes as showing motions or conveying both the chain connectivity... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_50520490" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Looking at proteins is an active process of interpretation and selection, emphasizing some features and deleting others. Multiple representations are needed, for such purposes as showing motions or conveying both the chain connectivity and the three-dimensional shape simultaneously. In studying and comparing protein structures, ideas are suggested about the determinants of tertiary structure and of folding (e.g., that Greek key #3 barrels may fold up two strands at a time). The design and synthesis of new proteins "from scratch" provides a route toward the experimental testing of such ideas. It has also been a fruitful new perspective from which to look at structures, requiring such things as statistics on very narrowly defined structural categories and explicit attention to "negative design" criteria that actively block unwanted alternatives (e.g., reverse topology of a helix bundle, or edge-to-edge aggregation ofs heets). Recently, the field of protein design has produced a rather unexpected general result: apparently we do indeed know enough to successfully design proteins that fold into approximately correct structures, but not enough to design unique, native-like structures. The degree of order varies considerably, but even the best designed material shows multiple conformations by NMR, more similar to a "molten globule" folding intermediate than to a well ordered native tertiary structure. In response to this conclusion, we are now working on systems that test useful questions with approximate structures (such as determining which factors most influence the choice of helix-bundle topology) and also analyzing how natural proteins achieve unique core conformations (e.g., for side chains on the interior side of a (3 sheet, illustrated in the kinemages).</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/50520490" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="11383e6c55fe2538b332341dd2a67fc3" rel="nofollow" data-download="{"attachment_id":68472743,"asset_id":50520490,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/68472743/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="165528325" href="https://independent.academia.edu/KimKitzler">Kim Kitzler</a><script data-card-contents-for-user="165528325" type="text/json">{"id":165528325,"first_name":"Kim","last_name":"Kitzler","domain_name":"independent","page_name":"KimKitzler","display_name":"Kim Kitzler","profile_url":"https://independent.academia.edu/KimKitzler?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_50520490 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="50520490"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 50520490, container: ".js-paper-rank-work_50520490", }); 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Biophysical Society National Lecture, 1992","created_at":"2021-08-01T09:05:09.738-07:00","url":"https://www.academia.edu/50520490/Looking_at_proteins_representations_folding_packing_and_design_Biophysical_Society_National_Lecture_1992?f_ri=19156","dom_id":"work_50520490","summary":"Looking at proteins is an active process of interpretation and selection, emphasizing some features and deleting others. Multiple representations are needed, for such purposes as showing motions or conveying both the chain connectivity and the three-dimensional shape simultaneously. In studying and comparing protein structures, ideas are suggested about the determinants of tertiary structure and of folding (e.g., that Greek key #3 barrels may fold up two strands at a time). The design and synthesis of new proteins \"from scratch\" provides a route toward the experimental testing of such ideas. It has also been a fruitful new perspective from which to look at structures, requiring such things as statistics on very narrowly defined structural categories and explicit attention to \"negative design\" criteria that actively block unwanted alternatives (e.g., reverse topology of a helix bundle, or edge-to-edge aggregation ofs heets). Recently, the field of protein design has produced a rather unexpected general result: apparently we do indeed know enough to successfully design proteins that fold into approximately correct structures, but not enough to design unique, native-like structures. The degree of order varies considerably, but even the best designed material shows multiple conformations by NMR, more similar to a \"molten globule\" folding intermediate than to a well ordered native tertiary structure. In response to this conclusion, we are now working on systems that test useful questions with approximate structures (such as determining which factors most influence the choice of helix-bundle topology) and also analyzing how natural proteins achieve unique core conformations (e.g., for side chains on the interior side of a (3 sheet, illustrated in the kinemages).","downloadable_attachments":[{"id":68472743,"asset_id":50520490,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":165528325,"first_name":"Kim","last_name":"Kitzler","domain_name":"independent","page_name":"KimKitzler","display_name":"Kim Kitzler","profile_url":"https://independent.academia.edu/KimKitzler?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":120789,"name":"Drug Design","url":"https://www.academia.edu/Documents/in/Drug_Design?f_ri=19156"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation?f_ri=19156"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence?f_ri=19156"},{"id":1724844,"name":"Molecular Structure","url":"https://www.academia.edu/Documents/in/Molecular_Structure?f_ri=19156"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_47338008" data-work_id="47338008" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/47338008/A_New_Deformation_Model_of_Hard_%CE%B1_Keratin_Fibers_at_the_Nanometer_Scale_Implications_for_Hard_%CE%B1_Keratin_Intermediate_Filament_Mechanical_Properties">A New Deformation Model of Hard α-Keratin Fibers at the Nanometer Scale: Implications for Hard α-Keratin Intermediate Filament Mechanical Properties</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The mechanical behavior of human hair fibers is determined by the interactions between keratin proteins structured into microfibrils (hard ␣-keratin intermediate filaments), a protein sulfur-rich matrix (intermediate filaments associated... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_47338008" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The mechanical behavior of human hair fibers is determined by the interactions between keratin proteins structured into microfibrils (hard ␣-keratin intermediate filaments), a protein sulfur-rich matrix (intermediate filaments associated proteins), and water molecules. The structure of the microfibril-matrix assembly has already been fully characterized using electron microscopy and small-angle x-ray scattering on unstressed fibers. However, these results give only a static image of this assembly. To observe and characterize the deformation of the microfibrils and of the matrix, we have carried out time-resolved small-angle x-ray microdiffraction experiments on human hair fibers stretched at 45% relative humidity and in water. Three structural parameters were monitored and quantified: the 6.7-nm meridian arc, which is related to an axial separation between groups of molecules along the microfibrils, the microfibril's radius, and the packing distance between microfibrils. Using a surface lattice model of the microfibril, we have described its deformation as a combination of a sliding process and a molecular stretching process. The radial contraction of the matrix is also emphasized, reinforcing the hydrophilic gel nature hypothesis.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/47338008" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="42b8ca725093c231a7ed361fb3266d58" rel="nofollow" data-download="{"attachment_id":66482842,"asset_id":47338008,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/66482842/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="188290659" href="https://independent.academia.edu/LKreplak">Laurent Kreplak</a><script data-card-contents-for-user="188290659" type="text/json">{"id":188290659,"first_name":"Laurent","last_name":"Kreplak","domain_name":"independent","page_name":"LKreplak","display_name":"Laurent Kreplak","profile_url":"https://independent.academia.edu/LKreplak?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_47338008 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="47338008"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 47338008, container: ".js-paper-rank-work_47338008", }); 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The structure of the microfibril-matrix assembly has already been fully characterized using electron microscopy and small-angle x-ray scattering on unstressed fibers. However, these results give only a static image of this assembly. To observe and characterize the deformation of the microfibrils and of the matrix, we have carried out time-resolved small-angle x-ray microdiffraction experiments on human hair fibers stretched at 45% relative humidity and in water. Three structural parameters were monitored and quantified: the 6.7-nm meridian arc, which is related to an axial separation between groups of molecules along the microfibrils, the microfibril's radius, and the packing distance between microfibrils. Using a surface lattice model of the microfibril, we have described its deformation as a combination of a sliding process and a molecular stretching process. The radial contraction of the matrix is also emphasized, reinforcing the hydrophilic gel nature hypothesis.","downloadable_attachments":[{"id":66482842,"asset_id":47338008,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":188290659,"first_name":"Laurent","last_name":"Kreplak","domain_name":"independent","page_name":"LKreplak","display_name":"Laurent Kreplak","profile_url":"https://independent.academia.edu/LKreplak?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=19156","nofollow":true},{"id":10636,"name":"Small Angle X Ray Scattering","url":"https://www.academia.edu/Documents/in/Small_Angle_X_Ray_Scattering?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":56001,"name":"X Rays","url":"https://www.academia.edu/Documents/in/X_Rays?f_ri=19156"},{"id":95016,"name":"Lattice Beam Model","url":"https://www.academia.edu/Documents/in/Lattice_Beam_Model?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":158186,"name":"Time Resolved","url":"https://www.academia.edu/Documents/in/Time_Resolved?f_ri=19156"},{"id":166367,"name":"Protein structure","url":"https://www.academia.edu/Documents/in/Protein_structure?f_ri=19156"},{"id":230744,"name":"Relative Humidity","url":"https://www.academia.edu/Documents/in/Relative_Humidity?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":2724508,"name":"Mechanical Property","url":"https://www.academia.edu/Documents/in/Mechanical_Property?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_1618799" data-work_id="1618799" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/1618799/Physicochemical_and_biological_characterization_of_1E10_Anti_Idiotype_vaccine">Physicochemical and biological characterization of 1E10 Anti-Idiotype vaccine</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Background: 1E10 monoclonal antibody is a murine anti-idiotypic antibody that mimics N-glycolyl-GM3 gangliosides. This antibody has been tested as an anti-idiotypic cancer vaccine, adjuvated in Al(OH) 3 , in several clinical trials for... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_1618799" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Background: 1E10 monoclonal antibody is a murine anti-idiotypic antibody that mimics N-glycolyl-GM3 gangliosides. This antibody has been tested as an anti-idiotypic cancer vaccine, adjuvated in Al(OH) 3 , in several clinical trials for melanoma, breast, and lung cancer. During early clinical development this mAb was obtained in vivo from mice ascites fluid. Currently, the production process of 1E10 is being transferred from the in vivo to a bioreactor-based method.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/1618799" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="d704672a4433ead476f2059803a37169" rel="nofollow" data-download="{"attachment_id":30996688,"asset_id":1618799,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/30996688/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="999193" href="https://sld.academia.edu/AdolfoCastillo">Adolfo Castillo</a><script data-card-contents-for-user="999193" type="text/json">{"id":999193,"first_name":"Adolfo","last_name":"Castillo","domain_name":"sld","page_name":"AdolfoCastillo","display_name":"Adolfo Castillo","profile_url":"https://sld.academia.edu/AdolfoCastillo?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_1618799 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="1618799"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 1618799, container: ".js-paper-rank-work_1618799", }); 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This antibody has been tested as an anti-idiotypic cancer vaccine, adjuvated in Al(OH) 3 , in several clinical trials for melanoma, breast, and lung cancer. During early clinical development this mAb was obtained in vivo from mice ascites fluid. Currently, the production process of 1E10 is being transferred from the in vivo to a bioreactor-based method.","downloadable_attachments":[{"id":30996688,"asset_id":1618799,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":999193,"first_name":"Adolfo","last_name":"Castillo","domain_name":"sld","page_name":"AdolfoCastillo","display_name":"Adolfo Castillo","profile_url":"https://sld.academia.edu/AdolfoCastillo?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":48,"name":"Engineering","url":"https://www.academia.edu/Documents/in/Engineering?f_ri=19156","nofollow":true},{"id":522,"name":"Thermodynamics","url":"https://www.academia.edu/Documents/in/Thermodynamics?f_ri=19156","nofollow":true},{"id":531,"name":"Organic Chemistry","url":"https://www.academia.edu/Documents/in/Organic_Chemistry?f_ri=19156","nofollow":true},{"id":532,"name":"Physical 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u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/11753066/Role_of_the_Transmembrane_Potential_in_the_Membrane_Proton_Leak">Role of the Transmembrane Potential in the Membrane Proton Leak</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The molecular mechanism responsible for the regulation of the mitochondrial membrane proton conductance (G) is not clearly understood. This study investigates the role of the transmembrane potential (DJ m ) using planar membranes,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_11753066" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The molecular mechanism responsible for the regulation of the mitochondrial membrane proton conductance (G) is not clearly understood. This study investigates the role of the transmembrane potential (DJ m ) using planar membranes, reconstituted with purified uncoupling proteins (UCP1 and UCP2) and/or unsaturated FA. We show that high DJ m (similar to DJ m in mitochondrial State IV) significantly activates the protonophoric function of UCPs in the presence of FA. The proton conductance increases nonlinearly with DJ m . The application of DJ m up to 220 mV leads to the overriding of the protein inhibition at a constant ATP concentration. Both, the exposure of FA-containing bilayers to high DJ m and the increase of FA membrane concentration bring about the significant exponential G m increase, implying the contribution of FA in proton leak. Quantitative analysis of the energy barrier for the transport of FA anions in the presence and absence of protein suggests that FA À remain exposed to membrane lipids while crossing the UCP-containing membrane. We believe this study shows that UCPs and FA decrease DJ m more effectively if it is sufficiently high. Thus, the tight regulation of proton conductance and/or FA concentration by DJ m may be key in mitochondrial respiration and metabolism.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/11753066" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="58850e136166564988ff3593a8483266" rel="nofollow" data-download="{"attachment_id":46544054,"asset_id":11753066,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46544054/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="28861763" href="https://independent.academia.edu/ValeriBeck">Valeri Beck</a><script data-card-contents-for-user="28861763" type="text/json">{"id":28861763,"first_name":"Valeri","last_name":"Beck","domain_name":"independent","page_name":"ValeriBeck","display_name":"Valeri Beck","profile_url":"https://independent.academia.edu/ValeriBeck?f_ri=19156","photo":"https://0.academia-photos.com/28861763/20815221/20362331/s65_valeri.beck.jpg"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-11753066">+2</span><div class="hidden js-additional-users-11753066"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/OlafNinnemann">Olaf Ninnemann</a></span></div><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://vetmeduni.academia.edu/ElenaPohl">Elena Pohl</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-11753066'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-11753066').html(); 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We believe this study shows that UCPs and FA decrease DJ m more effectively if it is sufficiently high. Thus, the tight regulation of proton conductance and/or FA concentration by DJ m may be key in mitochondrial respiration and metabolism.","downloadable_attachments":[{"id":46544054,"asset_id":11753066,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":28861763,"first_name":"Valeri","last_name":"Beck","domain_name":"independent","page_name":"ValeriBeck","display_name":"Valeri Beck","profile_url":"https://independent.academia.edu/ValeriBeck?f_ri=19156","photo":"https://0.academia-photos.com/28861763/20815221/20362331/s65_valeri.beck.jpg"},{"id":38176455,"first_name":"Olaf","last_name":"Ninnemann","domain_name":"independent","page_name":"OlafNinnemann","display_name":"Olaf Ninnemann","profile_url":"https://independent.academia.edu/OlafNinnemann?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":14135489,"first_name":"Elena","last_name":"Pohl","domain_name":"vetmeduni","page_name":"ElenaPohl","display_name":"Elena Pohl","profile_url":"https://vetmeduni.academia.edu/ElenaPohl?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":5493,"name":"Nonlinear dynamics","url":"https://www.academia.edu/Documents/in/Nonlinear_dynamics?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":31084,"name":"Ion Channels","url":"https://www.academia.edu/Documents/in/Ion_Channels?f_ri=19156","nofollow":true},{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=19156","nofollow":true},{"id":37434,"name":"Quantitative analysis","url":"https://www.academia.edu/Documents/in/Quantitative_analysis?f_ri=19156"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":72314,"name":"Fatty acids","url":"https://www.academia.edu/Documents/in/Fatty_acids?f_ri=19156"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":486713,"name":"Fatty Acid","url":"https://www.academia.edu/Documents/in/Fatty_Acid?f_ri=19156"},{"id":641216,"name":"Quantitative Analysis","url":"https://www.academia.edu/Documents/in/Quantitative_Analysis-1?f_ri=19156"},{"id":669339,"name":"Mes","url":"https://www.academia.edu/Documents/in/Mes?f_ri=19156"},{"id":1027866,"name":"SLS","url":"https://www.academia.edu/Documents/in/SLS?f_ri=19156"},{"id":1137254,"name":"Hydrogen-Ion Concentration","url":"https://www.academia.edu/Documents/in/Hydrogen-Ion_Concentration?f_ri=19156"},{"id":1161031,"name":"Uncoupling Protein","url":"https://www.academia.edu/Documents/in/Uncoupling_Protein?f_ri=19156"},{"id":1202042,"name":"Electric Conductivity","url":"https://www.academia.edu/Documents/in/Electric_Conductivity?f_ri=19156"},{"id":1208793,"name":"Protons","url":"https://www.academia.edu/Documents/in/Protons?f_ri=19156"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=19156"},{"id":2445801,"name":"Mitochondrial Proteins","url":"https://www.academia.edu/Documents/in/Mitochondrial_Proteins?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_12834083" data-work_id="12834083" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/12834083/Characterization_of_Chlorobium_tepidum_Chlorosomes_A_Calculation_of_Bacteriochlorophyll_c_per_Chlorosome_and_Oligomer_Modeling">Characterization of Chlorobium tepidum Chlorosomes: A Calculation of Bacteriochlorophyll c per Chlorosome and Oligomer Modeling</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The bacteriochlorophyll (Bchl) c content and organization was determined for Chlorobium (Cb.) tepidum chlorosomes, the light-harvesting complexes from green photosynthetic bacteria, using fluorescence correlation spectroscopy and atomic... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_12834083" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The bacteriochlorophyll (Bchl) c content and organization was determined for Chlorobium (Cb.) tepidum chlorosomes, the light-harvesting complexes from green photosynthetic bacteria, using fluorescence correlation spectroscopy and atomic force microscopy. Single-chlorosome fluorescence data was analyzed in terms of the correlation of the fluorescence intensity with time. Using this technique, known as fluorescence correlation spectroscopy, chlorosomes were shown to have a hydrodynamic radius (Rh) of 25 6 3.2 nm. This technique was also used to determine the concentration of chlorosomes in a sample, and pigment extraction and quantitation was used to determine the molar concentration of Bchl c present. From these data, a number of ;215,000 6 80,000 Bchl c per chlorosome was determined. Homogeneity of the sample was further characterized by dynamic light scattering, giving a single population of particles with a hydrodynamic radius of 26.8 6 3.7 nm in the sample. Tapping-mode atomic force microscopy (TMAFM) was used to determine the x,y,z dimensions of chlorosomes present in the sample. The results of the TMAFM studies indicated that the average chlorosome dimensions for Cb. tepidum was 174 6 8.3 3 91.4 6 7.7 3 10.9 6 2.71 nm and an overall average volume 90,800 nm 3 for the chlorosomes was determined. The data collected from these experiments as well as a model for Bchl c aggregate dimensions was used to determine possible arrangements of Bchl c oligomers in the chlorosomes. The results obtained in this study have significant implications on chlorosome structure and architecture, and will allow a more thorough investigation of the energetics of photosynthetic light harvesting in green bacteria.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/12834083" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="b227a2911316c944a3ff722f523215c6" rel="nofollow" data-download="{"attachment_id":45903592,"asset_id":12834083,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/45903592/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="31936004" href="https://wustl.academia.edu/RobertBlankenship">Robert Blankenship</a><script data-card-contents-for-user="31936004" type="text/json">{"id":31936004,"first_name":"Robert","last_name":"Blankenship","domain_name":"wustl","page_name":"RobertBlankenship","display_name":"Robert Blankenship","profile_url":"https://wustl.academia.edu/RobertBlankenship?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_12834083 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="12834083"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 12834083, container: ".js-paper-rank-work_12834083", }); 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$(".js-view-count[data-work-id=12834083]").text(description); $(".js-view-count-work_12834083").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_12834083").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="12834083"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">16</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="13845" rel="nofollow" href="https://www.academia.edu/Documents/in/Time_Use">Time Use</a>, <script data-card-contents-for-ri="13845" type="text/json">{"id":13845,"name":"Time Use","url":"https://www.academia.edu/Documents/in/Time_Use?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="24373" rel="nofollow" href="https://www.academia.edu/Documents/in/Atomic_Force_Microscopy">Atomic Force Microscopy</a>, <script data-card-contents-for-ri="24373" type="text/json">{"id":24373,"name":"Atomic Force Microscopy","url":"https://www.academia.edu/Documents/in/Atomic_Force_Microscopy?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="44380" rel="nofollow" href="https://www.academia.edu/Documents/in/Fluorescence_Correlation_Spectroscopy">Fluorescence Correlation Spectroscopy</a><script data-card-contents-for-ri="44380" type="text/json">{"id":44380,"name":"Fluorescence Correlation Spectroscopy","url":"https://www.academia.edu/Documents/in/Fluorescence_Correlation_Spectroscopy?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=12834083]'), work: {"id":12834083,"title":"Characterization of Chlorobium tepidum Chlorosomes: A Calculation of Bacteriochlorophyll c per Chlorosome and Oligomer Modeling","created_at":"2015-06-06T12:44:58.731-07:00","url":"https://www.academia.edu/12834083/Characterization_of_Chlorobium_tepidum_Chlorosomes_A_Calculation_of_Bacteriochlorophyll_c_per_Chlorosome_and_Oligomer_Modeling?f_ri=19156","dom_id":"work_12834083","summary":"The bacteriochlorophyll (Bchl) c content and organization was determined for Chlorobium (Cb.) tepidum chlorosomes, the light-harvesting complexes from green photosynthetic bacteria, using fluorescence correlation spectroscopy and atomic force microscopy. Single-chlorosome fluorescence data was analyzed in terms of the correlation of the fluorescence intensity with time. Using this technique, known as fluorescence correlation spectroscopy, chlorosomes were shown to have a hydrodynamic radius (Rh) of 25 6 3.2 nm. This technique was also used to determine the concentration of chlorosomes in a sample, and pigment extraction and quantitation was used to determine the molar concentration of Bchl c present. From these data, a number of ;215,000 6 80,000 Bchl c per chlorosome was determined. Homogeneity of the sample was further characterized by dynamic light scattering, giving a single population of particles with a hydrodynamic radius of 26.8 6 3.7 nm in the sample. Tapping-mode atomic force microscopy (TMAFM) was used to determine the x,y,z dimensions of chlorosomes present in the sample. The results of the TMAFM studies indicated that the average chlorosome dimensions for Cb. tepidum was 174 6 8.3 3 91.4 6 7.7 3 10.9 6 2.71 nm and an overall average volume 90,800 nm 3 for the chlorosomes was determined. The data collected from these experiments as well as a model for Bchl c aggregate dimensions was used to determine possible arrangements of Bchl c oligomers in the chlorosomes. The results obtained in this study have significant implications on chlorosome structure and architecture, and will allow a more thorough investigation of the energetics of photosynthetic light harvesting in green bacteria.","downloadable_attachments":[{"id":45903592,"asset_id":12834083,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":31936004,"first_name":"Robert","last_name":"Blankenship","domain_name":"wustl","page_name":"RobertBlankenship","display_name":"Robert Blankenship","profile_url":"https://wustl.academia.edu/RobertBlankenship?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":13845,"name":"Time Use","url":"https://www.academia.edu/Documents/in/Time_Use?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":24373,"name":"Atomic Force Microscopy","url":"https://www.academia.edu/Documents/in/Atomic_Force_Microscopy?f_ri=19156","nofollow":true},{"id":44380,"name":"Fluorescence Correlation Spectroscopy","url":"https://www.academia.edu/Documents/in/Fluorescence_Correlation_Spectroscopy?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":69542,"name":"Computer Simulation","url":"https://www.academia.edu/Documents/in/Computer_Simulation?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":142451,"name":"Dynamic Light Scattering","url":"https://www.academia.edu/Documents/in/Dynamic_Light_Scattering?f_ri=19156"},{"id":153168,"name":"Data Collection","url":"https://www.academia.edu/Documents/in/Data_Collection?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":965027,"name":"Subcellular Fractions","url":"https://www.academia.edu/Documents/in/Subcellular_Fractions?f_ri=19156"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=19156"},{"id":1275947,"name":"Light Harvesting","url":"https://www.academia.edu/Documents/in/Light_Harvesting?f_ri=19156"},{"id":1412232,"name":"Refractometry","url":"https://www.academia.edu/Documents/in/Refractometry?f_ri=19156"},{"id":1590415,"name":"Chlorobium","url":"https://www.academia.edu/Documents/in/Chlorobium?f_ri=19156"},{"id":1809037,"name":"Dimerization","url":"https://www.academia.edu/Documents/in/Dimerization?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_13525936" data-work_id="13525936" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/13525936/Action_Potential_Collision_in_Nerves">Action Potential Collision in Nerves</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">reproduce the complexity of arborization. We used the larval class IV sensory neuron in Drosophila as the model cell to approach this question. As class IV neurons display self-similarity over a range scales, the first key morphological... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_13525936" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">reproduce the complexity of arborization. We used the larval class IV sensory neuron in Drosophila as the model cell to approach this question. As class IV neurons display self-similarity over a range scales, the first key morphological parameter we use to study them is their fractal dimension. The fractal dimension of a neuron is a measure of its complexity and has been used to distinguish between classes of neurons. The second morphological parameter of a neuron involves realizing that such a branching structure can be viewed as a binary tree in which neuronal branching points are the nodes. The structure of interest here is the distribution of node depths, where the depth of a node is the number of other nodes between it and the root (i.e., the cell body) on the tree. Using both analytical techniques and in silico simulations, we made three findings. 1) The fractal dimension was always a monotonically increasing function of the neuron's maximal depth. 2) The observed Gaussian node-depth distributions are achievable via a termination rule in which the probability of branch termination is a sigmoidal function of node depth. 3) The observed nodedepth distributions can be qualitatively accounted for by an "inheritance rule", whereby each daughter segment inherits morphological information from its mother segment.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/13525936" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="c480ecd3169424d7083dbb7a5d84111e" rel="nofollow" data-download="{"attachment_id":45241112,"asset_id":13525936,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/45241112/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32724749" href="https://nbi.academia.edu/RimaBudvytyte">Rima Budvytyte</a><script data-card-contents-for-user="32724749" type="text/json">{"id":32724749,"first_name":"Rima","last_name":"Budvytyte","domain_name":"nbi","page_name":"RimaBudvytyte","display_name":"Rima Budvytyte","profile_url":"https://nbi.academia.edu/RimaBudvytyte?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_13525936 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="13525936"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 13525936, container: ".js-paper-rank-work_13525936", }); 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$(".js-view-count[data-work-id=13525936]").text(description); $(".js-view-count-work_13525936").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_13525936").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="13525936"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">4</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a>, <script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="260118" rel="nofollow" href="https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES">CHEMICAL SCIENCES</a><script data-card-contents-for-ri="260118" type="text/json">{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=13525936]'), work: {"id":13525936,"title":"Action Potential Collision in Nerves","created_at":"2015-07-02T00:16:52.003-07:00","url":"https://www.academia.edu/13525936/Action_Potential_Collision_in_Nerves?f_ri=19156","dom_id":"work_13525936","summary":"reproduce the complexity of arborization. We used the larval class IV sensory neuron in Drosophila as the model cell to approach this question. As class IV neurons display self-similarity over a range scales, the first key morphological parameter we use to study them is their fractal dimension. The fractal dimension of a neuron is a measure of its complexity and has been used to distinguish between classes of neurons. The second morphological parameter of a neuron involves realizing that such a branching structure can be viewed as a binary tree in which neuronal branching points are the nodes. The structure of interest here is the distribution of node depths, where the depth of a node is the number of other nodes between it and the root (i.e., the cell body) on the tree. Using both analytical techniques and in silico simulations, we made three findings. 1) The fractal dimension was always a monotonically increasing function of the neuron's maximal depth. 2) The observed Gaussian node-depth distributions are achievable via a termination rule in which the probability of branch termination is a sigmoidal function of node depth. 3) The observed nodedepth distributions can be qualitatively accounted for by an \"inheritance rule\", whereby each daughter segment inherits morphological information from its mother segment.","downloadable_attachments":[{"id":45241112,"asset_id":13525936,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32724749,"first_name":"Rima","last_name":"Budvytyte","domain_name":"nbi","page_name":"RimaBudvytyte","display_name":"Rima Budvytyte","profile_url":"https://nbi.academia.edu/RimaBudvytyte?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_24477344" data-work_id="24477344" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/24477344/A_Theoretical_Model_of_Slow_Wave_Regulation_Using_Voltage_Dependent_Synthesis_of_Inositol_1_4_5_Trisphosphate">A Theoretical Model of Slow Wave Regulation Using Voltage-Dependent Synthesis of Inositol 1,4,5-Trisphosphate</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">A qualitative mathematical model is presented that examines membrane potential feedback on synthesis of inositol 1,4,5-trisphosphate (IP 3 ), and its role in generation and modulation of slow waves. Previous experimental studies indicate... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_24477344" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">A qualitative mathematical model is presented that examines membrane potential feedback on synthesis of inositol 1,4,5-trisphosphate (IP 3 ), and its role in generation and modulation of slow waves. Previous experimental studies indicate that slow waves show voltage dependence, and this is likely to result through membrane potential modulation of IP 3 . It is proposed that the observed response of the tissue to current pulse, pulse train, and maintained current injection can be explained by changes in IP 3 , modulated through a voltage-IP 3 feedback loop. Differences underlying the tissue responses to current injections of opposite polarities are shown to be due to the sequence of events following such currents. Results from this model are consistent with experimental findings and provide further understanding of these experimental observations. Specifically, we find that membrane potential can induce, abolish, and modulate slow wave frequency by altering the excitability of the tissue through the voltage-IP 3 feedback loop.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/24477344" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="0dd35b0a9fcc0264d9e0b653be1da46a" rel="nofollow" data-download="{"attachment_id":44811180,"asset_id":24477344,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/44811180/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="47077852" href="https://independent.academia.edu/DirkHelden">Dirk Helden</a><script data-card-contents-for-user="47077852" type="text/json">{"id":47077852,"first_name":"Dirk","last_name":"Helden","domain_name":"independent","page_name":"DirkHelden","display_name":"Dirk Helden","profile_url":"https://independent.academia.edu/DirkHelden?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_24477344 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="24477344"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 24477344, container: ".js-paper-rank-work_24477344", }); 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Previous experimental studies indicate that slow waves show voltage dependence, and this is likely to result through membrane potential modulation of IP 3 . It is proposed that the observed response of the tissue to current pulse, pulse train, and maintained current injection can be explained by changes in IP 3 , modulated through a voltage-IP 3 feedback loop. Differences underlying the tissue responses to current injections of opposite polarities are shown to be due to the sequence of events following such currents. Results from this model are consistent with experimental findings and provide further understanding of these experimental observations. Specifically, we find that membrane potential can induce, abolish, and modulate slow wave frequency by altering the excitability of the tissue through the voltage-IP 3 feedback loop.","downloadable_attachments":[{"id":44811180,"asset_id":24477344,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":47077852,"first_name":"Dirk","last_name":"Helden","domain_name":"independent","page_name":"DirkHelden","display_name":"Dirk Helden","profile_url":"https://independent.academia.edu/DirkHelden?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true},{"id":2007,"name":"Electrophysiology","url":"https://www.academia.edu/Documents/in/Electrophysiology?f_ri=19156","nofollow":true},{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=19156","nofollow":true},{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":65171,"name":"Smooth muscle","url":"https://www.academia.edu/Documents/in/Smooth_muscle?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":215075,"name":"Experimental Study","url":"https://www.academia.edu/Documents/in/Experimental_Study?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":291387,"name":"Mathematical Model","url":"https://www.academia.edu/Documents/in/Mathematical_Model?f_ri=19156"},{"id":343667,"name":"Theoretical Models","url":"https://www.academia.edu/Documents/in/Theoretical_Models?f_ri=19156"},{"id":413195,"name":"Time Factors","url":"https://www.academia.edu/Documents/in/Time_Factors?f_ri=19156"},{"id":614190,"name":"Feedback loop","url":"https://www.academia.edu/Documents/in/Feedback_loop?f_ri=19156"},{"id":887736,"name":"Membrane Potential","url":"https://www.academia.edu/Documents/in/Membrane_Potential?f_ri=19156"},{"id":1154248,"name":"Theoretical Model","url":"https://www.academia.edu/Documents/in/Theoretical_Model?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_14128692 coauthored" data-work_id="14128692" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/14128692/Regulation_Of_The_Acetylcholine_Receptor_Function_By_Thyroid_Hormones">Regulation Of The Acetylcholine Receptor Function By Thyroid Hormones</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/14128692" data-share-source="work_strip" 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itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33123284" href="https://independent.academia.edu/YomarieRivera">Yomarie Rivera</a><script data-card-contents-for-user="33123284" type="text/json">{"id":33123284,"first_name":"Yomarie","last_name":"Rivera","domain_name":"independent","page_name":"YomarieRivera","display_name":"Yomarie Rivera","profile_url":"https://independent.academia.edu/YomarieRivera?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-14128692">+2</span><div class="hidden js-additional-users-14128692"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/LydiaMiranda">Lydia Miranda</a></span></div><div><span itemscope="itemscope" 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href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a>, <script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="260118" rel="nofollow" href="https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES">CHEMICAL SCIENCES</a><script data-card-contents-for-ri="260118" type="text/json">{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=14128692]'), work: {"id":14128692,"title":"Regulation Of The Acetylcholine Receptor Function By Thyroid Hormones","created_at":"2015-07-16T13:15:23.586-07:00","url":"https://www.academia.edu/14128692/Regulation_Of_The_Acetylcholine_Receptor_Function_By_Thyroid_Hormones?f_ri=19156","dom_id":"work_14128692","summary":null,"downloadable_attachments":[{"id":44578326,"asset_id":14128692,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33123284,"first_name":"Yomarie","last_name":"Rivera","domain_name":"independent","page_name":"YomarieRivera","display_name":"Yomarie Rivera","profile_url":"https://independent.academia.edu/YomarieRivera?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":33282146,"first_name":"Lydia","last_name":"Miranda","domain_name":"independent","page_name":"LydiaMiranda","display_name":"Lydia Miranda","profile_url":"https://independent.academia.edu/LydiaMiranda?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":6977094,"first_name":"Legier","last_name":"Rojas","domain_name":"uccaribe","page_name":"LegierRojas","display_name":"Legier Rojas","profile_url":"https://uccaribe.academia.edu/LegierRojas?f_ri=19156","photo":"https://0.academia-photos.com/6977094/2739417/3191342/s65_legier.rojas.jpg"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_21845313" data-work_id="21845313" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/21845313/Dehydron_A_Structurally_Encoded_Signal_for_Protein_Interaction">Dehydron: A Structurally Encoded Signal for Protein Interaction</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">We introduce a quantifiable structural motif, called dehydron, that is shown to be central to protein-protein interactions. A dehydron is a defectively packed backbone hydrogen bond suggesting preformed monomeric structure whose Coulomb... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_21845313" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">We introduce a quantifiable structural motif, called dehydron, that is shown to be central to protein-protein interactions. A dehydron is a defectively packed backbone hydrogen bond suggesting preformed monomeric structure whose Coulomb energy is highly sensitive to binding-induced water exclusion. Such preformed hydrogen bonds are effectively adhesive, since water removal from their vicinity contributes to their stability. At the structural level, a significant correlation is established between dehydrons and sites for protein complexation, with the HIV-1 capsid protein P24 complexed with antibody light-chain FAB25.3 providing the most dramatic correlation. Furthermore, the number of dehydrons in homologous similar-fold proteins from different species is shown to be a signature of proteomic complexity. The techniques are then applied to higher levels of organization: The formation of the capsid and its organization in picornaviruses correlates strongly with the distribution of dehydrons on the rim of the virus unit. Furthermore, antibody contacts and crystal contacts may be assigned to dehydrons still prevalent after the capsid has been assembled. The implications of the dehydron as an encoded signal in proteomics, bioinformatics, and inhibitor drug design are emphasized.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/21845313" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="471e71c18d5c03e8c8a7b9c3294cf0de" rel="nofollow" data-download="{"attachment_id":42589889,"asset_id":21845313,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42589889/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="3351608" href="https://colbas.academia.edu/ArielFernandez">Ariel Fernandez</a><script data-card-contents-for-user="3351608" type="text/json">{"id":3351608,"first_name":"Ariel","last_name":"Fernandez","domain_name":"colbas","page_name":"ArielFernandez","display_name":"Ariel Fernandez","profile_url":"https://colbas.academia.edu/ArielFernandez?f_ri=19156","photo":"https://0.academia-photos.com/3351608/1123259/2920838/s65_ariel.fernandez.png"}</script></span></span></li><li class="js-paper-rank-work_21845313 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="21845313"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 21845313, container: ".js-paper-rank-work_21845313", }); });</script></li><li class="js-percentile-work_21845313 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 21845313; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_21845313"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_21845313 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="21845313"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 21845313; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=21845313]").text(description); $(".js-view-count-work_21845313").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_21845313").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="21845313"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">22</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="502" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysics">Biophysics</a>, <script data-card-contents-for-ri="502" type="text/json">{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="2215" rel="nofollow" href="https://www.academia.edu/Documents/in/Water">Water</a>, <script data-card-contents-for-ri="2215" type="text/json">{"id":2215,"name":"Water","url":"https://www.academia.edu/Documents/in/Water?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="31264" rel="nofollow" href="https://www.academia.edu/Documents/in/Protein_Engineering">Protein Engineering</a><script data-card-contents-for-ri="31264" type="text/json">{"id":31264,"name":"Protein Engineering","url":"https://www.academia.edu/Documents/in/Protein_Engineering?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=21845313]'), work: {"id":21845313,"title":"Dehydron: A Structurally Encoded Signal for Protein Interaction","created_at":"2016-02-11T12:57:28.030-08:00","url":"https://www.academia.edu/21845313/Dehydron_A_Structurally_Encoded_Signal_for_Protein_Interaction?f_ri=19156","dom_id":"work_21845313","summary":"We introduce a quantifiable structural motif, called dehydron, that is shown to be central to protein-protein interactions. A dehydron is a defectively packed backbone hydrogen bond suggesting preformed monomeric structure whose Coulomb energy is highly sensitive to binding-induced water exclusion. Such preformed hydrogen bonds are effectively adhesive, since water removal from their vicinity contributes to their stability. At the structural level, a significant correlation is established between dehydrons and sites for protein complexation, with the HIV-1 capsid protein P24 complexed with antibody light-chain FAB25.3 providing the most dramatic correlation. Furthermore, the number of dehydrons in homologous similar-fold proteins from different species is shown to be a signature of proteomic complexity. The techniques are then applied to higher levels of organization: The formation of the capsid and its organization in picornaviruses correlates strongly with the distribution of dehydrons on the rim of the virus unit. Furthermore, antibody contacts and crystal contacts may be assigned to dehydrons still prevalent after the capsid has been assembled. The implications of the dehydron as an encoded signal in proteomics, bioinformatics, and inhibitor drug design are emphasized.","downloadable_attachments":[{"id":42589889,"asset_id":21845313,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":3351608,"first_name":"Ariel","last_name":"Fernandez","domain_name":"colbas","page_name":"ArielFernandez","display_name":"Ariel Fernandez","profile_url":"https://colbas.academia.edu/ArielFernandez?f_ri=19156","photo":"https://0.academia-photos.com/3351608/1123259/2920838/s65_ariel.fernandez.png"}],"research_interests":[{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true},{"id":2215,"name":"Water","url":"https://www.academia.edu/Documents/in/Water?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":31264,"name":"Protein Engineering","url":"https://www.academia.edu/Documents/in/Protein_Engineering?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":50487,"name":"Protein-Protein Interaction","url":"https://www.academia.edu/Documents/in/Protein-Protein_Interaction?f_ri=19156"},{"id":53293,"name":"Software","url":"https://www.academia.edu/Documents/in/Software?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":120789,"name":"Drug Design","url":"https://www.academia.edu/Documents/in/Drug_Design?f_ri=19156"},{"id":240148,"name":"Hydrogen Bond","url":"https://www.academia.edu/Documents/in/Hydrogen_Bond?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":296798,"name":"Hydrogen Bonding","url":"https://www.academia.edu/Documents/in/Hydrogen_Bonding?f_ri=19156"},{"id":300832,"name":"Protein Complex Detection","url":"https://www.academia.edu/Documents/in/Protein_Complex_Detection?f_ri=19156"},{"id":323803,"name":"Protein Interaction","url":"https://www.academia.edu/Documents/in/Protein_Interaction?f_ri=19156"},{"id":343667,"name":"Theoretical Models","url":"https://www.academia.edu/Documents/in/Theoretical_Models?f_ri=19156"},{"id":372917,"name":"Protein Secondary Structure Prediction","url":"https://www.academia.edu/Documents/in/Protein_Secondary_Structure_Prediction?f_ri=19156"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation?f_ri=19156"},{"id":890379,"name":"Rhinovirus","url":"https://www.academia.edu/Documents/in/Rhinovirus?f_ri=19156"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=19156"},{"id":1035050,"name":"Proteome","url":"https://www.academia.edu/Documents/in/Proteome?f_ri=19156"},{"id":1248637,"name":"Capsid Protein","url":"https://www.academia.edu/Documents/in/Capsid_Protein?f_ri=19156"},{"id":1312081,"name":"Light chain","url":"https://www.academia.edu/Documents/in/Light_chain?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_18746097 coauthored" data-work_id="18746097" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/18746097/Structure_of_the_Mycobacterium_Tuberculosis_Virulence_Factor_Rv0899_ompATb_">Structure of the Mycobacterium Tuberculosis Virulence Factor Rv0899 (ompATb)</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Exciting progress has been made recently in biophysical techniques that allow optical manipulation and measurement for single molecules at subnanometer scale as they undergo conformational transitions in real time. However, a serious... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_18746097" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Exciting progress has been made recently in biophysical techniques that allow optical manipulation and measurement for single molecules at subnanometer scale as they undergo conformational transitions in real time. However, a serious problem that could limit the future application of this technique is the photo damage to biological molecules brought by intense laser irradiation. The stateof-the-art high resolution optical tweezers instrument utilizes lasers that operate at 1064 nm, which coincides with the absorption of molecular oxygen in water. As a consequence, reactive oxygen species are generated during experiments that irreversibly modify the chemical structures of molecules under study. To solve this problem, we have constructed an optical tweezers instrument using a new generation high power diode laser that operates at 830 nm. Molecular oxygen has no absorption at this wavelength. We show that the choice of this laser not only eliminated photo damage associated with reactive oxygen species, the instrument also gained a faster frequency response, which stems from the overlap between trapping laser wavelength and the peak absorption of silicon photodetectors. Moreover, the sample temperature during experiments is much better controlled due to negligible absorption of water at 830 nm. All these advantages could significantly benefit future application of this single molecule technique in biological studies. We present our results from this instrument, and the status of spatial resolution for single molecule manipulation. Holographic optical tweezers (HOTs), in which a Spatial Light Modulator is used to change the phase pattern of the laser light, enable the manipulation in three dimensions of many particles simultaneously. This can be used for the probing of extended structures such as cells and extended protein networks. To allow for quantitative force measurements, the HOT traps need to be calibrated. However, nanometer-scale position modulations are introduced by the Spatial Light Modulator. In power spectral analysis, modulations at specific frequencies and drift can be readily identified in the spectrum and omitted before analysis, making this the preferred method of calibration for our HOTs. We use high-speed camera imaging for position detection of multiple trapped particles simultaneously, from which we obtain power spectra with 1.25 kHz bandwidth. For stiff traps, however, blur due to image integration time affects the detected particle positions significantly. Taking the effects of blur, aliasing and position detection error into account, as put forward by Wong and Halvorsen [Opt. Express 14, 12517, 2006], we are able to obtain the corner frequency f c of the power spectrum for stiff traps with f c up to 3.5 kHz. We demonstrate the utility of our calibration approach by measuring the force-extension curve for 4-micrometer-long DNA. Recent studies of kinetic behavior of binding and insertion of diphtheria toxin translocation domain (DTT) into lipid membranes [Kyrychenko et al. Biochemistry 2009, 48:7584] revealed the presence of several interfacial intermediates on the insertion pathway leading from soluble W-state to transmembrane T-state. It has been found that an intermediate interfacial I-state can be trapped in membranes with low content of anionic lipids (10%), while in membranes of greater anionic lipid content, another pH-dependent transition results in the formation of the insertion-competent state and subsequent transmembrane insertion. In this work we applied fluorescence correlation spectros-copy (FCS) to determine the free energy (DG) stabilizing final transmembrane and interfacial intermediate states. To avoid aggregation of DTT and to chaperone its membrane insertion, the FCS measurements were performed in the presence of fluorinated surfactants FTAC-C6. Our results indicate that the free energy of binding (DG) to lipid vesicles with formation of trapped interfacial intermediate state is about À8 kcal/mole, and this DG value does not change with pH, while the DG difference between transmembrane state and the interfacial state ranges from À1.5O-4 kcal/mole depending on membrane lipid composition and pH of media. Our results confirm the interface-directed model of spontaneous insertion of non-constitutive membrane proteins and provide an important benchmark for future measurements of DG stabilizing the structure of constitutive membrane proteins. The spontaneous folding of outer membrane proteins (OMPs) into lipid vesicles provides a means to study the determinants, kinetics, and thermodynamics of membrane protein folding in manipulatable systems modeling the native lipid environment. This information increases our ability to understand and utilize membrane proteins, but it remains sparse, with direct lipid refolding reported for fewer than a dozen unique OMPs. We present the spontaneous refolding of recombinant Opa proteins into lipid vesicles, with a systematic investigation of the impact protein and lipid bilayer variables have on the folding. Opa proteins are eight-stranded b-barreled monomeric integral outer membrane proteins found in the bacterial pathogens N. gonorrhoeae and N. meningitides. There are at least 26 characterized Opa proteins, nearly identical in sequence, but varying in three extracellular loops. In vivo, these proteins interact with specific human host cell receptors to breach the plasma membrane and gain entry to targeted human cells. The basis for host-receptor specificity is not well understood but is determined by the variable extracellular loops. These loops also play a role in folding. The b-sheets of Opa variants OpaI and OpaA are nearly identical in sequence, but OpaI refolds in DMPC vesicles while OpaA does not. These variants therefore provide a natural system to probe protein folding determinants. The effects of lipid composition (in particular both head group and chain length), buffer pH, ionic strength, and temperature on refolding have been characterized for these Opa variants. Ultimately, reconstitution into lipid bilayers required the matching of hydrophobic thicknesses as well as optimization of parameters mediating electrostatic interactions between the protein and lipids used. The reconstituted systems provide a new model in the study of membrane protein folding, with an exploration of refolding parameters that may be applicable to additional OMP-lipid systems.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/18746097" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="04d241a5666b1b922e7f5fc3c401cd20" rel="nofollow" data-download="{"attachment_id":40232856,"asset_id":18746097,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/40232856/download_file?st=MTczOTg1NTM5Miw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="38819656" href="https://independent.academia.edu/PeterTeriete">Peter Teriete</a><script data-card-contents-for-user="38819656" type="text/json">{"id":38819656,"first_name":"Peter","last_name":"Teriete","domain_name":"independent","page_name":"PeterTeriete","display_name":"Peter Teriete","profile_url":"https://independent.academia.edu/PeterTeriete?f_ri=19156","photo":"https://0.academia-photos.com/38819656/10756358/12006774/s65_peter.teriete.jpg"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-18746097">+1</span><div class="hidden js-additional-users-18746097"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/LeighPlesniak">Leigh Plesniak</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-18746097'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-18746097').html(); 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However, a serious problem that could limit the future application of this technique is the photo damage to biological molecules brought by intense laser irradiation. The stateof-the-art high resolution optical tweezers instrument utilizes lasers that operate at 1064 nm, which coincides with the absorption of molecular oxygen in water. As a consequence, reactive oxygen species are generated during experiments that irreversibly modify the chemical structures of molecules under study. To solve this problem, we have constructed an optical tweezers instrument using a new generation high power diode laser that operates at 830 nm. Molecular oxygen has no absorption at this wavelength. We show that the choice of this laser not only eliminated photo damage associated with reactive oxygen species, the instrument also gained a faster frequency response, which stems from the overlap between trapping laser wavelength and the peak absorption of silicon photodetectors. Moreover, the sample temperature during experiments is much better controlled due to negligible absorption of water at 830 nm. All these advantages could significantly benefit future application of this single molecule technique in biological studies. We present our results from this instrument, and the status of spatial resolution for single molecule manipulation. Holographic optical tweezers (HOTs), in which a Spatial Light Modulator is used to change the phase pattern of the laser light, enable the manipulation in three dimensions of many particles simultaneously. This can be used for the probing of extended structures such as cells and extended protein networks. To allow for quantitative force measurements, the HOT traps need to be calibrated. However, nanometer-scale position modulations are introduced by the Spatial Light Modulator. In power spectral analysis, modulations at specific frequencies and drift can be readily identified in the spectrum and omitted before analysis, making this the preferred method of calibration for our HOTs. We use high-speed camera imaging for position detection of multiple trapped particles simultaneously, from which we obtain power spectra with 1.25 kHz bandwidth. For stiff traps, however, blur due to image integration time affects the detected particle positions significantly. Taking the effects of blur, aliasing and position detection error into account, as put forward by Wong and Halvorsen [Opt. Express 14, 12517, 2006], we are able to obtain the corner frequency f c of the power spectrum for stiff traps with f c up to 3.5 kHz. We demonstrate the utility of our calibration approach by measuring the force-extension curve for 4-micrometer-long DNA. Recent studies of kinetic behavior of binding and insertion of diphtheria toxin translocation domain (DTT) into lipid membranes [Kyrychenko et al. Biochemistry 2009, 48:7584] revealed the presence of several interfacial intermediates on the insertion pathway leading from soluble W-state to transmembrane T-state. It has been found that an intermediate interfacial I-state can be trapped in membranes with low content of anionic lipids (10%), while in membranes of greater anionic lipid content, another pH-dependent transition results in the formation of the insertion-competent state and subsequent transmembrane insertion. In this work we applied fluorescence correlation spectros-copy (FCS) to determine the free energy (DG) stabilizing final transmembrane and interfacial intermediate states. To avoid aggregation of DTT and to chaperone its membrane insertion, the FCS measurements were performed in the presence of fluorinated surfactants FTAC-C6. Our results indicate that the free energy of binding (DG) to lipid vesicles with formation of trapped interfacial intermediate state is about À8 kcal/mole, and this DG value does not change with pH, while the DG difference between transmembrane state and the interfacial state ranges from À1.5O-4 kcal/mole depending on membrane lipid composition and pH of media. Our results confirm the interface-directed model of spontaneous insertion of non-constitutive membrane proteins and provide an important benchmark for future measurements of DG stabilizing the structure of constitutive membrane proteins. The spontaneous folding of outer membrane proteins (OMPs) into lipid vesicles provides a means to study the determinants, kinetics, and thermodynamics of membrane protein folding in manipulatable systems modeling the native lipid environment. This information increases our ability to understand and utilize membrane proteins, but it remains sparse, with direct lipid refolding reported for fewer than a dozen unique OMPs. We present the spontaneous refolding of recombinant Opa proteins into lipid vesicles, with a systematic investigation of the impact protein and lipid bilayer variables have on the folding. Opa proteins are eight-stranded b-barreled monomeric integral outer membrane proteins found in the bacterial pathogens N. gonorrhoeae and N. meningitides. There are at least 26 characterized Opa proteins, nearly identical in sequence, but varying in three extracellular loops. In vivo, these proteins interact with specific human host cell receptors to breach the plasma membrane and gain entry to targeted human cells. The basis for host-receptor specificity is not well understood but is determined by the variable extracellular loops. These loops also play a role in folding. The b-sheets of Opa variants OpaI and OpaA are nearly identical in sequence, but OpaI refolds in DMPC vesicles while OpaA does not. These variants therefore provide a natural system to probe protein folding determinants. The effects of lipid composition (in particular both head group and chain length), buffer pH, ionic strength, and temperature on refolding have been characterized for these Opa variants. Ultimately, reconstitution into lipid bilayers required the matching of hydrophobic thicknesses as well as optimization of parameters mediating electrostatic interactions between the protein and lipids used. The reconstituted systems provide a new model in the study of membrane protein folding, with an exploration of refolding parameters that may be applicable to additional OMP-lipid systems.","downloadable_attachments":[{"id":40232856,"asset_id":18746097,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":38819656,"first_name":"Peter","last_name":"Teriete","domain_name":"independent","page_name":"PeterTeriete","display_name":"Peter Teriete","profile_url":"https://independent.academia.edu/PeterTeriete?f_ri=19156","photo":"https://0.academia-photos.com/38819656/10756358/12006774/s65_peter.teriete.jpg"},{"id":39004937,"first_name":"Leigh","last_name":"Plesniak","domain_name":"independent","page_name":"LeighPlesniak","display_name":"Leigh Plesniak","profile_url":"https://independent.academia.edu/LeighPlesniak?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":68318,"name":"Mycobacterium tuberculosis","url":"https://www.academia.edu/Documents/in/Mycobacterium_tuberculosis?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":587939,"name":"Virulence factor","url":"https://www.academia.edu/Documents/in/Virulence_factor?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_18255309" data-work_id="18255309" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/18255309/The_Route_and_Mechanism_of_Uncoupled_Current_Flow_through_Na_K_ATPase_Pumps_Lacking_the_Two_COOH_Terminal_Tyrosines">The Route and Mechanism of Uncoupled Current Flow through Na/K-ATPase Pumps Lacking the Two COOH-Terminal Tyrosines</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Moreover, we found that under a sufficiently strong torque in the opposite direction of ATP hydrolytic rotations, it rotated in the opposite direction, or the ATP synthetic direction, in a stepwise manner. The torque necessary for... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_18255309" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Moreover, we found that under a sufficiently strong torque in the opposite direction of ATP hydrolytic rotations, it rotated in the opposite direction, or the ATP synthetic direction, in a stepwise manner. The torque necessary for rotations in the synthetic direction times 120 was nearly equal to˛0 0˛1 /4 under various conditions except for conditions at sufficiently low ADP concentrations.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/18255309" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="9c5e88304a2f92f93f70f151fafc3045" rel="nofollow" data-download="{"attachment_id":39957938,"asset_id":18255309,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/39957938/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="38242115" href="https://oxford.academia.edu/NatasciaVedovato">Natascia Vedovato</a><script data-card-contents-for-user="38242115" type="text/json">{"id":38242115,"first_name":"Natascia","last_name":"Vedovato","domain_name":"oxford","page_name":"NatasciaVedovato","display_name":"Natascia Vedovato","profile_url":"https://oxford.academia.edu/NatasciaVedovato?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_18255309 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="18255309"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 18255309, container: ".js-paper-rank-work_18255309", }); });</script></li><li class="js-percentile-work_18255309 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 18255309; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_18255309"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_18255309 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="18255309"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 18255309; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=18255309]").text(description); $(".js-view-count-work_18255309").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_18255309").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="18255309"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">4</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a>, <script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="260118" rel="nofollow" href="https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES">CHEMICAL SCIENCES</a><script data-card-contents-for-ri="260118" type="text/json">{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=18255309]'), work: {"id":18255309,"title":"The Route and Mechanism of Uncoupled Current Flow through Na/K-ATPase Pumps Lacking the Two COOH-Terminal Tyrosines","created_at":"2015-11-12T23:16:21.472-08:00","url":"https://www.academia.edu/18255309/The_Route_and_Mechanism_of_Uncoupled_Current_Flow_through_Na_K_ATPase_Pumps_Lacking_the_Two_COOH_Terminal_Tyrosines?f_ri=19156","dom_id":"work_18255309","summary":"Moreover, we found that under a sufficiently strong torque in the opposite direction of ATP hydrolytic rotations, it rotated in the opposite direction, or the ATP synthetic direction, in a stepwise manner. The torque necessary for rotations in the synthetic direction times 120 was nearly equal to˛0 0˛1 /4 under various conditions except for conditions at sufficiently low ADP concentrations.","downloadable_attachments":[{"id":39957938,"asset_id":18255309,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":38242115,"first_name":"Natascia","last_name":"Vedovato","domain_name":"oxford","page_name":"NatasciaVedovato","display_name":"Natascia Vedovato","profile_url":"https://oxford.academia.edu/NatasciaVedovato?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_68113898" data-work_id="68113898" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" rel="nofollow" href="https://www.academia.edu/68113898/Amyloid_%CE%B2_peptide_insertion_in_liposomes_containing_GM1_cholesterol_domains">Amyloid β-peptide insertion in liposomes containing GM1-cholesterol domains</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Neuronal membrane damage is related to the early impairments appearing in... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_68113898" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Neuronal membrane damage is related to the early impairments appearing in Alzheimer&amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;#39;s disease due to the interaction of the amyloid β-peptide (Aβ) with the phospholipid bilayer. In particular, the ganglioside GM1, present with cholesterol in lipid rafts, seems to be able to initiate Aβ aggregation on membrane. We studied the thermodynamic and structural effects of the presence of GM1 on the interaction between Aβ and liposomes, a good membrane model system. Isothermal Titration Calorimetry highlighted the importance of the presence of GM1 in recruiting monomeric Aβ toward the lipid bilayer. Light and Small Angle X-ray Scattering revealed a different pattern for GM1 containing liposomes, both before and after interaction with Aβ. The results suggest that the interaction with GM1 brings to insertion of Aβ in the bilayer, producing a structural perturbation down to the internal layers of the liposome, as demonstrated by the obtained electron density profiles.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/68113898" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="212350395" href="https://independent.academia.edu/dariospigolon">dario spigolon</a><script data-card-contents-for-user="212350395" type="text/json">{"id":212350395,"first_name":"dario","last_name":"spigolon","domain_name":"independent","page_name":"dariospigolon","display_name":"dario spigolon","profile_url":"https://independent.academia.edu/dariospigolon?f_ri=19156","photo":"https://0.academia-photos.com/212350395/71483825/59929230/s65_dario.spigolon.png"}</script></span></span></li><li class="js-paper-rank-work_68113898 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="68113898"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 68113898, container: ".js-paper-rank-work_68113898", }); 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In particular, the ganglioside GM1, present with cholesterol in lipid rafts, seems to be able to initiate Aβ aggregation on membrane. We studied the thermodynamic and structural effects of the presence of GM1 on the interaction between Aβ and liposomes, a good membrane model system. Isothermal Titration Calorimetry highlighted the importance of the presence of GM1 in recruiting monomeric Aβ toward the lipid bilayer. Light and Small Angle X-ray Scattering revealed a different pattern for GM1 containing liposomes, both before and after interaction with Aβ. The results suggest that the interaction with GM1 brings to insertion of Aβ in the bilayer, producing a structural perturbation down to the internal layers of the liposome, as demonstrated by the obtained electron density profiles.","downloadable_attachments":[],"ordered_authors":[{"id":212350395,"first_name":"dario","last_name":"spigolon","domain_name":"independent","page_name":"dariospigolon","display_name":"dario spigolon","profile_url":"https://independent.academia.edu/dariospigolon?f_ri=19156","photo":"https://0.academia-photos.com/212350395/71483825/59929230/s65_dario.spigolon.png"}],"research_interests":[{"id":522,"name":"Thermodynamics","url":"https://www.academia.edu/Documents/in/Thermodynamics?f_ri=19156","nofollow":true},{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical 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u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_62533591" data-work_id="62533591" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/62533591/How_Chlamydomonas_Keeps_Track_of_the_Light_Once_It_Has_Reached_the_Right_Phototactic_Orientation">How Chlamydomonas Keeps Track of the Light Once It Has Reached the Right Phototactic Orientation</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">By using a real-time assay that allows measurement of the phototactic orientation of the unicellular alga Chlamydomonas with millisecond time resolution, it can be shown that single photons not only induce transient direction changes but... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_62533591" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">By using a real-time assay that allows measurement of the phototactic orientation of the unicellular alga Chlamydomonas with millisecond time resolution, it can be shown that single photons not only induce transient direction changes but that fluence rates as low as 1 photon cell(-1) ...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/62533591" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3f491bd832be687db68b6dc2bec191bc" rel="nofollow" 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}); });</script></span><script>$(function() { $(".js-view-count-work_62533591").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="62533591"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">13</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="53293" rel="nofollow" href="https://www.academia.edu/Documents/in/Software">Software</a>, <script data-card-contents-for-ri="53293" type="text/json">{"id":53293,"name":"Software","url":"https://www.academia.edu/Documents/in/Software?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="62244" rel="nofollow" href="https://www.academia.edu/Documents/in/Video_microscopy">Video microscopy</a><script data-card-contents-for-ri="62244" type="text/json">{"id":62244,"name":"Video microscopy","url":"https://www.academia.edu/Documents/in/Video_microscopy?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: 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Results","url":"https://www.academia.edu/Documents/in/Reproducibility_of_Results?f_ri=19156"},{"id":1126161,"name":"Chlamydomonas Reinhardtii","url":"https://www.academia.edu/Documents/in/Chlamydomonas_Reinhardtii?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_56498264" data-work_id="56498264" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/56498264/Quicker_than_Quick_Correlative_Optical_Tweezers_Fluorescence_Microscopy_CTFM_for_the_Study_of_Short_Lived_Metabolic_Processes">Quicker than Quick: Correlative Optical Tweezers-Fluorescence Microscopy (CTFM) for the Study of Short-Lived Metabolic Processes</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">squamous cell carcinoma cell lines (SCC-74B and SCC-74A, respectively). The in vitro metabolic state was manipulated by changes in temperature, substrate concentration, plating density, and by the use of metabolic uncouplers and... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_56498264" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">squamous cell carcinoma cell lines (SCC-74B and SCC-74A, respectively). The in vitro metabolic state was manipulated by changes in temperature, substrate concentration, plating density, and by the use of metabolic uncouplers and inhibitors. Changes in the metabolic state were clearly evident in both lifetime and phasor histograms as well as fluorescence intensity within each cell line. In addition, SCC-74B and À74A could clearly be distinguished as SCC-74B displayed a reduced fluorescence intensity dynamic range compared to SCC-74A. Surprisingly, variation in the endogenous fluorescence signatures of nuclear and cytoplasmic regions were also evident. Recently, we have successfully applied this technique to assess UV exposed cells and intact mouse skin, adapting the measurement and analysis protocols to provide a rapid quantitative metabolic profile. Various fluorescent signals from the skin have been identified and separated from metabolic signals by their unique spectral and lifetime and phasor signatures.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/56498264" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="85be4cd5c237004464fd2b79889afaab" rel="nofollow" data-download="{"attachment_id":71855674,"asset_id":56498264,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/71855674/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="41860620" href="https://independent.academia.edu/GerritSitters">Gerrit Sitters</a><script data-card-contents-for-user="41860620" type="text/json">{"id":41860620,"first_name":"Gerrit","last_name":"Sitters","domain_name":"independent","page_name":"GerritSitters","display_name":"Gerrit Sitters","profile_url":"https://independent.academia.edu/GerritSitters?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_56498264 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="56498264"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 56498264, container: ".js-paper-rank-work_56498264", }); 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The in vitro metabolic state was manipulated by changes in temperature, substrate concentration, plating density, and by the use of metabolic uncouplers and inhibitors. Changes in the metabolic state were clearly evident in both lifetime and phasor histograms as well as fluorescence intensity within each cell line. In addition, SCC-74B and À74A could clearly be distinguished as SCC-74B displayed a reduced fluorescence intensity dynamic range compared to SCC-74A. Surprisingly, variation in the endogenous fluorescence signatures of nuclear and cytoplasmic regions were also evident. Recently, we have successfully applied this technique to assess UV exposed cells and intact mouse skin, adapting the measurement and analysis protocols to provide a rapid quantitative metabolic profile. Various fluorescent signals from the skin have been identified and separated from metabolic signals by their unique spectral and lifetime and phasor signatures.","downloadable_attachments":[{"id":71855674,"asset_id":56498264,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":41860620,"first_name":"Gerrit","last_name":"Sitters","domain_name":"independent","page_name":"GerritSitters","display_name":"Gerrit Sitters","profile_url":"https://independent.academia.edu/GerritSitters?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_49161406" data-work_id="49161406" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/49161406/An_On_Chip_Pcr_Approach_Enabling_Cancer_Diagnosis">An On-Chip Pcr Approach Enabling Cancer Diagnosis</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/49161406" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="36304b3d189262524df5fb078e3e1cc2" rel="nofollow" data-download="{"attachment_id":67548870,"asset_id":49161406,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/67548870/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="159233142" href="https://stanford.academia.edu/SeungminPark">Seung-min Park</a><script data-card-contents-for-user="159233142" type="text/json">{"id":159233142,"first_name":"Seung-min","last_name":"Park","domain_name":"stanford","page_name":"SeungminPark","display_name":"Seung-min Park","profile_url":"https://stanford.academia.edu/SeungminPark?f_ri=19156","photo":"https://0.academia-photos.com/159233142/44603994/35057870/s65_seung-min.park.jpg"}</script></span></span></li><li class="js-paper-rank-work_49161406 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="49161406"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 49161406, container: ".js-paper-rank-work_49161406", }); 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They contribute to structural, biochemical, mechanical and electrical properties of the myocardium. Nonetheless, they are often... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_48214059" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Cardiac fibroblasts form one of the largest cell populations, in terms of cell numbers, in the heart. They contribute to structural, biochemical, mechanical and electrical properties of the myocardium. Nonetheless, they are often disregarded by in vivo and in vitro studies into cardiac function. This review summarizes our understanding of fibroblast origin and identity, their structural organization and role in myocardial architecture, as well as functional aspects related to cell signalling and electro-mechanical function in the heart.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/48214059" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="888517eb2ccaed8f7931f8a03d19c155" rel="nofollow" data-download="{"attachment_id":66943277,"asset_id":48214059,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/66943277/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="189356623" href="https://independent.academia.edu/MaiteGarcia49">Maite Garcia</a><script data-card-contents-for-user="189356623" type="text/json">{"id":189356623,"first_name":"Maite","last_name":"Garcia","domain_name":"independent","page_name":"MaiteGarcia49","display_name":"Maite Garcia","profile_url":"https://independent.academia.edu/MaiteGarcia49?f_ri=19156","photo":"https://0.academia-photos.com/189356623/52626392/40739851/s65_maite.garcia.jpeg"}</script></span></span></li><li class="js-paper-rank-work_48214059 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="48214059"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 48214059, container: ".js-paper-rank-work_48214059", }); 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$(".js-view-count[data-work-id=48214059]").text(description); $(".js-view-count-work_48214059").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_48214059").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="48214059"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">13</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="3284" rel="nofollow" href="https://www.academia.edu/Documents/in/Bacteriology">Bacteriology</a>, <script data-card-contents-for-ri="3284" type="text/json">{"id":3284,"name":"Bacteriology","url":"https://www.academia.edu/Documents/in/Bacteriology?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="4366" rel="nofollow" href="https://www.academia.edu/Documents/in/Cardiovascular">Cardiovascular</a>, <script data-card-contents-for-ri="4366" type="text/json">{"id":4366,"name":"Cardiovascular","url":"https://www.academia.edu/Documents/in/Cardiovascular?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="8089" rel="nofollow" href="https://www.academia.edu/Documents/in/Virology">Virology</a>, <script data-card-contents-for-ri="8089" type="text/json">{"id":8089,"name":"Virology","url":"https://www.academia.edu/Documents/in/Virology?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="16062" rel="nofollow" href="https://www.academia.edu/Documents/in/Starch">Starch</a><script data-card-contents-for-ri="16062" type="text/json">{"id":16062,"name":"Starch","url":"https://www.academia.edu/Documents/in/Starch?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=48214059]'), work: {"id":48214059,"title":"Structural and Functional Characterization of DUF1471 Domains of Salmonella Proteins SrfN, YdgH/SssB, and YahO","created_at":"2021-05-04T05:21:30.171-07:00","url":"https://www.academia.edu/48214059/Structural_and_Functional_Characterization_of_DUF1471_Domains_of_Salmonella_Proteins_SrfN_YdgH_SssB_and_YahO?f_ri=19156","dom_id":"work_48214059","summary":"Cardiac fibroblasts form one of the largest cell populations, in terms of cell numbers, in the heart. They contribute to structural, biochemical, mechanical and electrical properties of the myocardium. Nonetheless, they are often disregarded by in vivo and in vitro studies into cardiac function. This review summarizes our understanding of fibroblast origin and identity, their structural organization and role in myocardial architecture, as well as functional aspects related to cell signalling and electro-mechanical function in the heart.","downloadable_attachments":[{"id":66943277,"asset_id":48214059,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":189356623,"first_name":"Maite","last_name":"Garcia","domain_name":"independent","page_name":"MaiteGarcia49","display_name":"Maite Garcia","profile_url":"https://independent.academia.edu/MaiteGarcia49?f_ri=19156","photo":"https://0.academia-photos.com/189356623/52626392/40739851/s65_maite.garcia.jpeg"}],"research_interests":[{"id":3284,"name":"Bacteriology","url":"https://www.academia.edu/Documents/in/Bacteriology?f_ri=19156","nofollow":true},{"id":4366,"name":"Cardiovascular","url":"https://www.academia.edu/Documents/in/Cardiovascular?f_ri=19156","nofollow":true},{"id":8089,"name":"Virology","url":"https://www.academia.edu/Documents/in/Virology?f_ri=19156","nofollow":true},{"id":16062,"name":"Starch","url":"https://www.academia.edu/Documents/in/Starch?f_ri=19156","nofollow":true},{"id":18520,"name":"Biological Chemistry","url":"https://www.academia.edu/Documents/in/Biological_Chemistry?f_ri=19156"},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156"},{"id":178906,"name":"Nucleic Acids","url":"https://www.academia.edu/Documents/in/Nucleic_Acids?f_ri=19156"},{"id":204870,"name":"Modified Starch","url":"https://www.academia.edu/Documents/in/Modified_Starch?f_ri=19156"},{"id":220780,"name":"PLoS one","url":"https://www.academia.edu/Documents/in/PLoS_one?f_ri=19156"},{"id":276821,"name":"Molecular sciences","url":"https://www.academia.edu/Documents/in/Molecular_sciences?f_ri=19156"},{"id":298508,"name":"Sweet Potato","url":"https://www.academia.edu/Documents/in/Sweet_Potato?f_ri=19156"},{"id":328449,"name":"Molecules","url":"https://www.academia.edu/Documents/in/Molecules?f_ri=19156"},{"id":894295,"name":"Gelatinitation of Starch","url":"https://www.academia.edu/Documents/in/Gelatinitation_of_Starch?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_36013386" data-work_id="36013386" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/36013386/A_Quantitative_Assessment_Of_Selective_Pharmacological_Inhibition_Of_Serca_In_Isolated_Rabbit_Working_Hearts">A Quantitative Assessment Of Selective Pharmacological Inhibition Of Serca In Isolated Rabbit Working Hearts</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">and is detrimental to myocardial function. We previously demonstrated that high levels of peroxynitrite decrease myocardial contraction by reducing phospholamban (PLB) phosphorylation through a protein phosphatase-dependent mechanism.... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_36013386" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">and is detrimental to myocardial function. We previously demonstrated that high levels of peroxynitrite decrease myocardial contraction by reducing phospholamban (PLB) phosphorylation through a protein phosphatase-dependent mechanism. However, we did not examine the direct effect of peroxynitrite on protein phosphatase activity in the myocardium or the specific protein phosphatase which is activated. Here we test: 1.) the effect of SIN-1 (peroxynitrite donor) on protein phosphatase activity in whole heart homogenates using a colorimetric assay, and 2.) the effect of SIN-1 on the interaction of PLB with protein phosphatase 1 (PP1) and protein phosphatase 2a (PP2a) using co-immunoprecipitation. SIN-1 induced a 63% increase in total protein phosphatase activity (1.650.2 vs. 2.650.3 nmol/min/mg, p<0.05 vs. Control), which was abolished with specific PP1/PP2a inhibition using okadaic acid (1.450.2 nmol/min/mg, p<0.05 vs. SIN-1). Since okadaic acid prevented the effects of SIN-1, we next examined the effect of SIN-1 on the interaction of PLB with PP1 and PP2a. SIN-1 increased the interaction of PLB with PP2a by 350% (0.65 0.3 vs. 2.750.7 A.U., p<0.05 vs. Control), but had no effect on the interaction with PP1. The peroxynitrite scavenger, urate, prevented both the SIN-1-induced increase in protein phosphatase activity and the interaction of PLB with PP2a, thus implicating peroxynitrite as the causal species. The results of this study provide further insight into the mechanism through which high levels of peroxynitrite serve to decrease PLB phosphorylation and myocardial contraction. Therefore, increased peroxynitrite production may play a key role in heart failure where protein phosphatase activity is increased and PLB phosphorylation is decreased, ultimately leading to contractile dysfunction.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/36013386" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="e598caf50ce93364f4f1f45acb89fd6b" rel="nofollow" data-download="{"attachment_id":55899812,"asset_id":36013386,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/55899812/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="38559379" href="https://glasgow.academia.edu/ChristopherLoughrey">Christopher Loughrey</a><script data-card-contents-for-user="38559379" type="text/json">{"id":38559379,"first_name":"Christopher","last_name":"Loughrey","domain_name":"glasgow","page_name":"ChristopherLoughrey","display_name":"Christopher Loughrey","profile_url":"https://glasgow.academia.edu/ChristopherLoughrey?f_ri=19156","photo":"https://0.academia-photos.com/38559379/16979508/19084565/s65_christopher.loughrey.jpg"}</script></span></span></li><li class="js-paper-rank-work_36013386 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="36013386"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 36013386, container: ".js-paper-rank-work_36013386", }); 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We previously demonstrated that high levels of peroxynitrite decrease myocardial contraction by reducing phospholamban (PLB) phosphorylation through a protein phosphatase-dependent mechanism. However, we did not examine the direct effect of peroxynitrite on protein phosphatase activity in the myocardium or the specific protein phosphatase which is activated. Here we test: 1.) the effect of SIN-1 (peroxynitrite donor) on protein phosphatase activity in whole heart homogenates using a colorimetric assay, and 2.) the effect of SIN-1 on the interaction of PLB with protein phosphatase 1 (PP1) and protein phosphatase 2a (PP2a) using co-immunoprecipitation. SIN-1 induced a 63% increase in total protein phosphatase activity (1.650.2 vs. 2.650.3 nmol/min/mg, p\u003c0.05 vs. Control), which was abolished with specific PP1/PP2a inhibition using okadaic acid (1.450.2 nmol/min/mg, p\u003c0.05 vs. SIN-1). Since okadaic acid prevented the effects of SIN-1, we next examined the effect of SIN-1 on the interaction of PLB with PP1 and PP2a. SIN-1 increased the interaction of PLB with PP2a by 350% (0.65 0.3 vs. 2.750.7 A.U., p\u003c0.05 vs. Control), but had no effect on the interaction with PP1. The peroxynitrite scavenger, urate, prevented both the SIN-1-induced increase in protein phosphatase activity and the interaction of PLB with PP2a, thus implicating peroxynitrite as the causal species. The results of this study provide further insight into the mechanism through which high levels of peroxynitrite serve to decrease PLB phosphorylation and myocardial contraction. Therefore, increased peroxynitrite production may play a key role in heart failure where protein phosphatase activity is increased and PLB phosphorylation is decreased, ultimately leading to contractile dysfunction.","downloadable_attachments":[{"id":55899812,"asset_id":36013386,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":38559379,"first_name":"Christopher","last_name":"Loughrey","domain_name":"glasgow","page_name":"ChristopherLoughrey","display_name":"Christopher Loughrey","profile_url":"https://glasgow.academia.edu/ChristopherLoughrey?f_ri=19156","photo":"https://0.academia-photos.com/38559379/16979508/19084565/s65_christopher.loughrey.jpg"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_34057483" data-work_id="34057483" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/34057483/Neutron_Reflectivity_Studies_of_the_Antimicrobial_Peptide_Maculatin_1_1_in_Supported_Lipid_Bilayers">Neutron Reflectivity Studies of the Antimicrobial Peptide Maculatin 1.1 in Supported Lipid Bilayers</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/34057483" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="cc6310843310b5c0f8ddc4867384a231" rel="nofollow" data-download="{"attachment_id":53994981,"asset_id":34057483,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" 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{"id":34057483,"title":"Neutron Reflectivity Studies of the Antimicrobial Peptide Maculatin 1.1 in Supported Lipid Bilayers","created_at":"2017-07-27T17:45:56.779-07:00","url":"https://www.academia.edu/34057483/Neutron_Reflectivity_Studies_of_the_Antimicrobial_Peptide_Maculatin_1_1_in_Supported_Lipid_Bilayers?f_ri=19156","dom_id":"work_34057483","summary":null,"downloadable_attachments":[{"id":53994981,"asset_id":34057483,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":46508975,"first_name":"david","last_name":"fernandez","domain_name":"independent","page_name":"davidfernandez116","display_name":"david fernandez","profile_url":"https://independent.academia.edu/davidfernandez116?f_ri=19156","photo":"https://0.academia-photos.com/46508975/17385376/17479920/s65_david.fernandez.jpg"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":220440,"name":"Antimicrobial Peptide","url":"https://www.academia.edu/Documents/in/Antimicrobial_Peptide?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":1145644,"name":"Lipid Bilayer","url":"https://www.academia.edu/Documents/in/Lipid_Bilayer?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_942458" data-work_id="942458" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/942458/Effect_of_sensor_domain_mutations_on_the_properties_of_voltage_gated_ion_channels_molecular_dynamics_studies_of_the_potassium_channel_Kv1_2">Effect of sensor domain mutations on the properties of voltage-gated ion channels: molecular dynamics studies of the potassium channel Kv1. 2</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The effects on the structural and functional properties of the Kv1.2 voltage-gated ion channel, caused by selective mutation of voltage sensor domain residues, have been investigated using classical molecular dynamics simulations.... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_942458" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The effects on the structural and functional properties of the Kv1.2 voltage-gated ion channel, caused by selective mutation of voltage sensor domain residues, have been investigated using classical molecular dynamics simulations. Following experiments that have identified mutations of voltage-gated ion channels involved in state-dependent omega currents, we observe for both the open and closed conformations of the Kv1.2 that specific mutations of S4 gating-charge residues destabilize the electrostatic network between helices of the voltage sensor domain, resulting in the formation of hydrophilic pathways linking the intra-and extracellular media. When such mutant channels are subject to transmembrane potentials, they conduct cations via these so-called ''omega pores.'' This study provides therefore further insight into the molecular mechanisms that lead to omega currents, which have been linked to certain channelopathies.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/942458" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="6695f5e5f818c718eeb9a770c9c78361" rel="nofollow" data-download="{"attachment_id":51155443,"asset_id":942458,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/51155443/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="701519" href="https://temple.academia.edu/LucieDelemotte">Lucie Delemotte</a><script data-card-contents-for-user="701519" type="text/json">{"id":701519,"first_name":"Lucie","last_name":"Delemotte","domain_name":"temple","page_name":"LucieDelemotte","display_name":"Lucie Delemotte","profile_url":"https://temple.academia.edu/LucieDelemotte?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_942458 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="942458"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 942458, container: ".js-paper-rank-work_942458", }); 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Following experiments that have identified mutations of voltage-gated ion channels involved in state-dependent omega currents, we observe for both the open and closed conformations of the Kv1.2 that specific mutations of S4 gating-charge residues destabilize the electrostatic network between helices of the voltage sensor domain, resulting in the formation of hydrophilic pathways linking the intra-and extracellular media. When such mutant channels are subject to transmembrane potentials, they conduct cations via these so-called ''omega pores.'' This study provides therefore further insight into the molecular mechanisms that lead to omega currents, which have been linked to certain channelopathies.","downloadable_attachments":[{"id":51155443,"asset_id":942458,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":701519,"first_name":"Lucie","last_name":"Delemotte","domain_name":"temple","page_name":"LucieDelemotte","display_name":"Lucie Delemotte","profile_url":"https://temple.academia.edu/LucieDelemotte?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2736,"name":"Molecular Dynamics Simulation","url":"https://www.academia.edu/Documents/in/Molecular_Dynamics_Simulation?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":49646,"name":"Protein Structure and Function","url":"https://www.academia.edu/Documents/in/Protein_Structure_and_Function?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation?f_ri=19156"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence?f_ri=19156"},{"id":894908,"name":"Amino Acid Substitution Rates","url":"https://www.academia.edu/Documents/in/Amino_Acid_Substitution_Rates?f_ri=19156"},{"id":1217930,"name":"Site-directed Mutagenesis","url":"https://www.academia.edu/Documents/in/Site-directed_Mutagenesis?f_ri=19156"},{"id":1242504,"name":"Molecular Dynamic Simulation","url":"https://www.academia.edu/Documents/in/Molecular_Dynamic_Simulation?f_ri=19156"},{"id":1451660,"name":"Static Electricity","url":"https://www.academia.edu/Documents/in/Static_Electricity?f_ri=19156"},{"id":1980640,"name":"State dependence","url":"https://www.academia.edu/Documents/in/State_dependence?f_ri=19156"},{"id":2045377,"name":"Functional Properties","url":"https://www.academia.edu/Documents/in/Functional_Properties?f_ri=19156"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_8682343 coauthored" data-work_id="8682343" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/8682343/Cholesterol_Organization_in_Membranes_at_Low_Concentrations_Effects_of_Curvature_Stress_and_Membrane_Thickness">Cholesterol Organization in Membranes at Low Concentrations: Effects of Curvature Stress and Membrane Thickness</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Cholesterol is often found distributed nonrandomly in domains in biological and model membranes and has been reported to be distributed heterogeneously among various intracellular membranes. Although a large body of literature exists on... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_8682343" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Cholesterol is often found distributed nonrandomly in domains in biological and model membranes and has been reported to be distributed heterogeneously among various intracellular membranes. Although a large body of literature exists on the organization of cholesterol in plasma membranes or membranes with high cholesterol content, very little is known about organization of cholesterol in membranes containing low amounts of cholesterol. Using a fluorescent cholesterol analog (25-[N-[(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-methyl]amino]-27-norcholesterol, or NBD-cholesterol), we have previously shown that cholesterol may exhibit local organization even at very low concentrations in membranes, which could possibly be attributable to transbilayer tail-to-tail dimers. This is supported by similar observations reported by other groups using cholesterol or dehydroergosterol, a naturally occurring fluorescent cholesterol analog which closely mimics cholesterol. In this paper, we have tested the basic features of cholesterol organization in membranes at low concentrations using spectral features of dehydroergosterol. More importantly, we have investigated the role of membrane surface curvature and thickness on transbilayer dimer arrangement of cholesterol using NBD-cholesterol. We find that dimerization is not favored in membranes with high curvature. However, cholesterol dimers are observed again if the curvature stress is relieved. Further, we have monitored the effect of membrane thickness on the dimerization process. Our results show that the dimerization process is stringently controlled by a narrow window of membrane thickness. Interestingly, this type of local organization of NBD-cholesterol at low concentrations is also observed in sphingomyelin-containing membranes. These results could be significant in membranes that have very low cholesterol content, such as the endoplasmic reticulum and the inner mitochondrial membrane, and in trafficking and sorting of cellular cholesterol.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/8682343" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="32a9aff0c90a71707c79c9a509bd5795" rel="nofollow" data-download="{"attachment_id":48021313,"asset_id":8682343,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/48021313/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="18174955" href="https://ccmb.academia.edu/RukminiRaju">Rukmini Raju</a><script data-card-contents-for-user="18174955" type="text/json">{"id":18174955,"first_name":"Rukmini","last_name":"Raju","domain_name":"ccmb","page_name":"RukminiRaju","display_name":"Rukmini Raju","profile_url":"https://ccmb.academia.edu/RukminiRaju?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-8682343">+1</span><div class="hidden js-additional-users-8682343"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/AmitabhaChattopadhyay1">Amitabha Chattopadhyay</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-8682343'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-8682343').html(); 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Although a large body of literature exists on the organization of cholesterol in plasma membranes or membranes with high cholesterol content, very little is known about organization of cholesterol in membranes containing low amounts of cholesterol. Using a fluorescent cholesterol analog (25-[N-[(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-methyl]amino]-27-norcholesterol, or NBD-cholesterol), we have previously shown that cholesterol may exhibit local organization even at very low concentrations in membranes, which could possibly be attributable to transbilayer tail-to-tail dimers. This is supported by similar observations reported by other groups using cholesterol or dehydroergosterol, a naturally occurring fluorescent cholesterol analog which closely mimics cholesterol. In this paper, we have tested the basic features of cholesterol organization in membranes at low concentrations using spectral features of dehydroergosterol. More importantly, we have investigated the role of membrane surface curvature and thickness on transbilayer dimer arrangement of cholesterol using NBD-cholesterol. We find that dimerization is not favored in membranes with high curvature. However, cholesterol dimers are observed again if the curvature stress is relieved. Further, we have monitored the effect of membrane thickness on the dimerization process. Our results show that the dimerization process is stringently controlled by a narrow window of membrane thickness. Interestingly, this type of local organization of NBD-cholesterol at low concentrations is also observed in sphingomyelin-containing membranes. These results could be significant in membranes that have very low cholesterol content, such as the endoplasmic reticulum and the inner mitochondrial membrane, and in trafficking and sorting of cellular cholesterol.","downloadable_attachments":[{"id":48021313,"asset_id":8682343,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":18174955,"first_name":"Rukmini","last_name":"Raju","domain_name":"ccmb","page_name":"RukminiRaju","display_name":"Rukmini Raju","profile_url":"https://ccmb.academia.edu/RukminiRaju?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":228378622,"first_name":"Amitabha","last_name":"Chattopadhyay","domain_name":"independent","page_name":"AmitabhaChattopadhyay1","display_name":"Amitabha Chattopadhyay","profile_url":"https://independent.academia.edu/AmitabhaChattopadhyay1?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":4377,"name":"Membranes","url":"https://www.academia.edu/Documents/in/Membranes?f_ri=19156","nofollow":true},{"id":18529,"name":"Fluorescent Dyes and Reagents","url":"https://www.academia.edu/Documents/in/Fluorescent_Dyes_and_Reagents?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":90514,"name":"Cholesterol","url":"https://www.academia.edu/Documents/in/Cholesterol?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum?f_ri=19156"},{"id":154672,"name":"Membrane Lipids","url":"https://www.academia.edu/Documents/in/Membrane_Lipids?f_ri=19156"},{"id":178351,"name":"Spectrophotometry","url":"https://www.academia.edu/Documents/in/Spectrophotometry?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":440924,"name":"Surface Properties","url":"https://www.academia.edu/Documents/in/Surface_Properties?f_ri=19156"},{"id":534568,"name":"High Cholesterol","url":"https://www.academia.edu/Documents/in/High_Cholesterol?f_ri=19156"},{"id":960467,"name":"Ergosterol","url":"https://www.academia.edu/Documents/in/Ergosterol?f_ri=19156"},{"id":1242344,"name":"Plasma Membrane","url":"https://www.academia.edu/Documents/in/Plasma_Membrane?f_ri=19156"},{"id":1809037,"name":"Dimerization","url":"https://www.academia.edu/Documents/in/Dimerization?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_27136252" data-work_id="27136252" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/27136252/%CE%B1_%CE%B1_Cross_Links_Increase_Fibrin_Fiber_Elasticity_and_Stiffness">α−α Cross-Links Increase Fibrin Fiber Elasticity and Stiffness</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Fibrin fibers, which are~100 nm in diameter, are the major structural component of a blood clot. The mechanical properties of single fibrin fibers determine the behavior of a blood clot and, thus, have a critical influence on heart... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_27136252" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Fibrin fibers, which are~100 nm in diameter, are the major structural component of a blood clot. The mechanical properties of single fibrin fibers determine the behavior of a blood clot and, thus, have a critical influence on heart attacks, strokes, and embolisms. Cross-linking is thought to fortify blood clots; though, the role of a-a cross-links in fibrin fiber assembly and their effect on the mechanical properties of single fibrin fibers are poorly understood. To address this knowledge gap, we used a combined fluorescence and atomic force microscope technique to determine the stiffness (modulus), extensibility, and elasticity of individual, uncross-linked, exclusively a-a cross-linked (gQ398N/Q399N/K406R fibrinogen variant), and completely cross-linked fibrin fibers. Exclusive a-a cross-linking results in 2.5Â stiffer and 1.5Â more elastic fibers, whereas full cross-linking results in 3.75Â stiffer, 1.2Â more elastic, but 1.2Â less extensible fibers, as compared to uncross-linked fibers. On the basis of these results and data from the literature, we propose a model in which the a-C region plays a significant role in inter-and intralinking of fibrin molecules and protofibrils, endowing fibrin fibers with increased stiffness and elasticity.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/27136252" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="d1774ecebef1fb4426445178fec40915" rel="nofollow" data-download="{"attachment_id":47385239,"asset_id":27136252,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/47385239/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="51157512" href="https://independent.academia.edu/MartinGuthold">Martin Guthold</a><script data-card-contents-for-user="51157512" type="text/json">{"id":51157512,"first_name":"Martin","last_name":"Guthold","domain_name":"independent","page_name":"MartinGuthold","display_name":"Martin Guthold","profile_url":"https://independent.academia.edu/MartinGuthold?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_27136252 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="27136252"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 27136252, container: ".js-paper-rank-work_27136252", }); 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$(".js-view-count[data-work-id=27136252]").text(description); $(".js-view-count-work_27136252").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_27136252").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="27136252"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">10</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="61095" rel="nofollow" href="https://www.academia.edu/Documents/in/Fibrin">Fibrin</a>, <script data-card-contents-for-ri="61095" type="text/json">{"id":61095,"name":"Fibrin","url":"https://www.academia.edu/Documents/in/Fibrin?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="69542" rel="nofollow" href="https://www.academia.edu/Documents/in/Computer_Simulation">Computer Simulation</a><script data-card-contents-for-ri="69542" type="text/json">{"id":69542,"name":"Computer Simulation","url":"https://www.academia.edu/Documents/in/Computer_Simulation?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=27136252]'), work: {"id":27136252,"title":"α−α Cross-Links Increase Fibrin Fiber Elasticity and Stiffness","created_at":"2016-07-20T12:30:30.612-07:00","url":"https://www.academia.edu/27136252/%CE%B1_%CE%B1_Cross_Links_Increase_Fibrin_Fiber_Elasticity_and_Stiffness?f_ri=19156","dom_id":"work_27136252","summary":"Fibrin fibers, which are~100 nm in diameter, are the major structural component of a blood clot. The mechanical properties of single fibrin fibers determine the behavior of a blood clot and, thus, have a critical influence on heart attacks, strokes, and embolisms. Cross-linking is thought to fortify blood clots; though, the role of a-a cross-links in fibrin fiber assembly and their effect on the mechanical properties of single fibrin fibers are poorly understood. To address this knowledge gap, we used a combined fluorescence and atomic force microscope technique to determine the stiffness (modulus), extensibility, and elasticity of individual, uncross-linked, exclusively a-a cross-linked (gQ398N/Q399N/K406R fibrinogen variant), and completely cross-linked fibrin fibers. Exclusive a-a cross-linking results in 2.5Â stiffer and 1.5Â more elastic fibers, whereas full cross-linking results in 3.75Â stiffer, 1.2Â more elastic, but 1.2Â less extensible fibers, as compared to uncross-linked fibers. On the basis of these results and data from the literature, we propose a model in which the a-C region plays a significant role in inter-and intralinking of fibrin molecules and protofibrils, endowing fibrin fibers with increased stiffness and elasticity.","downloadable_attachments":[{"id":47385239,"asset_id":27136252,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":51157512,"first_name":"Martin","last_name":"Guthold","domain_name":"independent","page_name":"MartinGuthold","display_name":"Martin Guthold","profile_url":"https://independent.academia.edu/MartinGuthold?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":61095,"name":"Fibrin","url":"https://www.academia.edu/Documents/in/Fibrin?f_ri=19156","nofollow":true},{"id":69542,"name":"Computer Simulation","url":"https://www.academia.edu/Documents/in/Computer_Simulation?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":350931,"name":"Mechanical Stress","url":"https://www.academia.edu/Documents/in/Mechanical_Stress?f_ri=19156"},{"id":586110,"name":"Elastic Modulus","url":"https://www.academia.edu/Documents/in/Elastic_Modulus?f_ri=19156"},{"id":973999,"name":"Tensile Strength","url":"https://www.academia.edu/Documents/in/Tensile_Strength?f_ri=19156"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_16021215 coauthored" data-work_id="16021215" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/16021215/A_Quantitative_Model_of_Thermal_Stabilization_and_Destabilization_of_Proteins_by_Ligands">A Quantitative Model of Thermal Stabilization and Destabilization of Proteins by Ligands</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Equilibrium binding ligands usually increase protein thermal stability by an amount proportional to the concentration and affinity of the ligand. High-throughput screening for the discovery of drug-like compounds uses an assay based on... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_16021215" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Equilibrium binding ligands usually increase protein thermal stability by an amount proportional to the concentration and affinity of the ligand. High-throughput screening for the discovery of drug-like compounds uses an assay based on thermal stabilization. The mathematical description of this stabilization is well developed, and the method is widely applicable to the characterization of ligand-protein binding equilibrium. However, numerous cases have been experimentally observed where equilibrium binding ligands destabilize proteins, i.e., diminish protein melting temperature by an amount proportional to the concentration and affinity of the ligand. Here, we present a thermodynamic model that describes ligand binding to the native and unfolded (denatured) protein states explaining the combined stabilization and destabilization effects. The model also explains nonsaturation and saturation effects on the protein melting temperature when the ligand concentration significantly exceeds the protein concentration. Several examples of the applicability of the model are presented, including specific sulfonamide binding to recombinant hCAII, peptide and ANS binding to the Polo-box domain of Plk1, and zinc ion binding to the recombinant porcine growth hormone. The same ligands may stabilize and destabilize different proteins, and the same proteins may be stabilized and destabilized by different ligands.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/16021215" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="15de3cb6c936a5c7067b73efb2b3a618" rel="nofollow" data-download="{"attachment_id":42783751,"asset_id":16021215,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42783751/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="35163350" href="https://independent.academia.edu/JelenaJachno">Jelena Jachno</a><script data-card-contents-for-user="35163350" type="text/json">{"id":35163350,"first_name":"Jelena","last_name":"Jachno","domain_name":"independent","page_name":"JelenaJachno","display_name":"Jelena Jachno","profile_url":"https://independent.academia.edu/JelenaJachno?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-16021215">+4</span><div class="hidden js-additional-users-16021215"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/JurgitaMatulien%C4%97">Jurgita Matulienė</a></span></div><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/JolantaTorresan">Jolanta Torresan</a></span></div><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/PiotrasCimmperman">Piotras Cimmperman</a></span></div><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/VladasBumelis">Vladas Bumelis</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-16021215'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-16021215').html(); 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container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_16021215 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="16021215"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 16021215; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=16021215]").text(description); $(".js-view-count-work_16021215").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_16021215").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="16021215"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">21</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="522" rel="nofollow" href="https://www.academia.edu/Documents/in/Thermodynamics">Thermodynamics</a>, <script data-card-contents-for-ri="522" type="text/json">{"id":522,"name":"Thermodynamics","url":"https://www.academia.edu/Documents/in/Thermodynamics?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="6811" rel="nofollow" href="https://www.academia.edu/Documents/in/Quantum_Theory">Quantum Theory</a>, <script data-card-contents-for-ri="6811" type="text/json">{"id":6811,"name":"Quantum Theory","url":"https://www.academia.edu/Documents/in/Quantum_Theory?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a><script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=16021215]'), work: {"id":16021215,"title":"A Quantitative Model of Thermal Stabilization and Destabilization of Proteins by Ligands","created_at":"2015-09-22T05:11:57.738-07:00","url":"https://www.academia.edu/16021215/A_Quantitative_Model_of_Thermal_Stabilization_and_Destabilization_of_Proteins_by_Ligands?f_ri=19156","dom_id":"work_16021215","summary":"Equilibrium binding ligands usually increase protein thermal stability by an amount proportional to the concentration and affinity of the ligand. High-throughput screening for the discovery of drug-like compounds uses an assay based on thermal stabilization. The mathematical description of this stabilization is well developed, and the method is widely applicable to the characterization of ligand-protein binding equilibrium. However, numerous cases have been experimentally observed where equilibrium binding ligands destabilize proteins, i.e., diminish protein melting temperature by an amount proportional to the concentration and affinity of the ligand. Here, we present a thermodynamic model that describes ligand binding to the native and unfolded (denatured) protein states explaining the combined stabilization and destabilization effects. The model also explains nonsaturation and saturation effects on the protein melting temperature when the ligand concentration significantly exceeds the protein concentration. Several examples of the applicability of the model are presented, including specific sulfonamide binding to recombinant hCAII, peptide and ANS binding to the Polo-box domain of Plk1, and zinc ion binding to the recombinant porcine growth hormone. The same ligands may stabilize and destabilize different proteins, and the same proteins may be stabilized and destabilized by different ligands.","downloadable_attachments":[{"id":42783751,"asset_id":16021215,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":35163350,"first_name":"Jelena","last_name":"Jachno","domain_name":"independent","page_name":"JelenaJachno","display_name":"Jelena Jachno","profile_url":"https://independent.academia.edu/JelenaJachno?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":38431920,"first_name":"Jurgita","last_name":"Matulienė","domain_name":"independent","page_name":"JurgitaMatulienė","display_name":"Jurgita Matulienė","profile_url":"https://independent.academia.edu/JurgitaMatulien%C4%97?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":35240230,"first_name":"Jolanta","last_name":"Torresan","domain_name":"independent","page_name":"JolantaTorresan","display_name":"Jolanta Torresan","profile_url":"https://independent.academia.edu/JolantaTorresan?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":35239019,"first_name":"Piotras","last_name":"Cimmperman","domain_name":"independent","page_name":"PiotrasCimmperman","display_name":"Piotras Cimmperman","profile_url":"https://independent.academia.edu/PiotrasCimmperman?f_ri=19156","photo":"https://0.academia-photos.com/35239019/18557815/18525734/s65_piotras.cimmperman.jpg"},{"id":38593589,"first_name":"Vladas","last_name":"Bumelis","domain_name":"independent","page_name":"VladasBumelis","display_name":"Vladas Bumelis","profile_url":"https://independent.academia.edu/VladasBumelis?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":522,"name":"Thermodynamics","url":"https://www.academia.edu/Documents/in/Thermodynamics?f_ri=19156","nofollow":true},{"id":6811,"name":"Quantum Theory","url":"https://www.academia.edu/Documents/in/Quantum_Theory?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":52562,"name":"Growth Hormone","url":"https://www.academia.edu/Documents/in/Growth_Hormone?f_ri=19156"},{"id":88745,"name":"High throughput screening","url":"https://www.academia.edu/Documents/in/High_throughput_screening?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":120297,"name":"Ligand Binding","url":"https://www.academia.edu/Documents/in/Ligand_Binding?f_ri=19156"},{"id":133177,"name":"Temperature","url":"https://www.academia.edu/Documents/in/Temperature?f_ri=19156"},{"id":158165,"name":"Zinc","url":"https://www.academia.edu/Documents/in/Zinc?f_ri=19156"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":389180,"name":"Thermal Stability","url":"https://www.academia.edu/Documents/in/Thermal_Stability?f_ri=19156"},{"id":419370,"name":"Swine","url":"https://www.academia.edu/Documents/in/Swine?f_ri=19156"},{"id":983317,"name":"Cell Cycle Proteins","url":"https://www.academia.edu/Documents/in/Cell_Cycle_Proteins?f_ri=19156"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=19156"},{"id":1186541,"name":"Protein Denaturation","url":"https://www.academia.edu/Documents/in/Protein_Denaturation?f_ri=19156"},{"id":1222191,"name":"Ligands","url":"https://www.academia.edu/Documents/in/Ligands?f_ri=19156"},{"id":1491514,"name":"*Hot Temperature","url":"https://www.academia.edu/Documents/in/_Hot_Temperature?f_ri=19156"},{"id":2104033,"name":"Melting Temperature","url":"https://www.academia.edu/Documents/in/Melting_Temperature?f_ri=19156"},{"id":2276570,"name":"Transition Temperature","url":"https://www.academia.edu/Documents/in/Transition_Temperature?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_17274416 coauthored" data-work_id="17274416" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/17274416/Mitochondrial_Protein_p32_Can_Accumulate_in_the_Nucleus">Mitochondrial Protein p32 Can Accumulate in the Nucleus</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/17274416" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="7cd38ba26ec2d1064e62f18c53f1c8ba" rel="nofollow" data-download="{"attachment_id":42275378,"asset_id":17274416,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42275378/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="37289965" href="https://uib.academia.edu/KarlAlbertBrokstad">Karl Albert Brokstad</a><script data-card-contents-for-user="37289965" type="text/json">{"id":37289965,"first_name":"Karl Albert","last_name":"Brokstad","domain_name":"uib","page_name":"KarlAlbertBrokstad","display_name":"Karl Albert 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InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="17274416"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 17274416; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=17274416]").text(description); $(".js-view-count-work_17274416").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_17274416").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="17274416"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">11</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="15719" rel="nofollow" href="https://www.academia.edu/Documents/in/Mitochondria">Mitochondria</a>, <script data-card-contents-for-ri="15719" type="text/json">{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="57808" rel="nofollow" href="https://www.academia.edu/Documents/in/Cell_line">Cell line</a>, <script data-card-contents-for-ri="57808" type="text/json">{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="112334" rel="nofollow" href="https://www.academia.edu/Documents/in/Methanol">Methanol</a><script data-card-contents-for-ri="112334" type="text/json">{"id":112334,"name":"Methanol","url":"https://www.academia.edu/Documents/in/Methanol?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=17274416]'), work: {"id":17274416,"title":"Mitochondrial Protein p32 Can Accumulate in the Nucleus","created_at":"2015-10-25T07:10:17.905-07:00","url":"https://www.academia.edu/17274416/Mitochondrial_Protein_p32_Can_Accumulate_in_the_Nucleus?f_ri=19156","dom_id":"work_17274416","summary":null,"downloadable_attachments":[{"id":42275378,"asset_id":17274416,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":37289965,"first_name":"Karl Albert","last_name":"Brokstad","domain_name":"uib","page_name":"KarlAlbertBrokstad","display_name":"Karl Albert Brokstad","profile_url":"https://uib.academia.edu/KarlAlbertBrokstad?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":36918397,"first_name":"Karl-henning","last_name":"Kalland","domain_name":"independent","page_name":"KarlhenningKalland","display_name":"Karl-henning Kalland","profile_url":"https://independent.academia.edu/KarlhenningKalland?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line?f_ri=19156","nofollow":true},{"id":112334,"name":"Methanol","url":"https://www.academia.edu/Documents/in/Methanol?f_ri=19156","nofollow":true},{"id":317801,"name":"Cell nucleus","url":"https://www.academia.edu/Documents/in/Cell_nucleus?f_ri=19156"},{"id":422325,"name":"HeLa cells","url":"https://www.academia.edu/Documents/in/HeLa_cells?f_ri=19156"},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection?f_ri=19156"},{"id":886461,"name":"Ribonucleoproteins","url":"https://www.academia.edu/Documents/in/Ribonucleoproteins?f_ri=19156"},{"id":1341094,"name":"Tissue Fixation","url":"https://www.academia.edu/Documents/in/Tissue_Fixation?f_ri=19156"},{"id":1557916,"name":"Nuclear Import","url":"https://www.academia.edu/Documents/in/Nuclear_Import?f_ri=19156"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_19220170" data-work_id="19220170" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/19220170/Anthracycline_gels">Anthracycline gels</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Anthracycline antibiotic; Thermally reversible gel; NMR, 'H-Gels have been prepared from aqueous solutions of anthracyclines by addition of salts. The gels are thixotropic and thermally reversible. They are stable for several months in... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_19220170" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Anthracycline antibiotic; Thermally reversible gel; NMR, 'H-Gels have been prepared from aqueous solutions of anthracyclines by addition of salts. The gels are thixotropic and thermally reversible. They are stable for several months in the refrigerator and for long times even at room temperature.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/19220170" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="170aa9733446a18b5747ae9d3a6f0ccb" rel="nofollow" data-download="{"attachment_id":40498534,"asset_id":19220170,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/40498534/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="39448500" href="https://independent.academia.edu/MauroGiustini">Mauro. 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The gels are thixotropic and thermally reversible. They are stable for several months in the refrigerator and for long times even at room temperature.","downloadable_attachments":[{"id":40498534,"asset_id":19220170,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":39448500,"first_name":"Mauro.","last_name":"Giustini","domain_name":"independent","page_name":"MauroGiustini","display_name":"Mauro. Giustini","profile_url":"https://independent.academia.edu/MauroGiustini?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true},{"id":974408,"name":"Physico chemical Properties","url":"https://www.academia.edu/Documents/in/Physico_chemical_Properties?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_69861411" data-work_id="69861411" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/69861411/Factors_Associated_with_Occupational_Stress_and_Their_Effects_on_Organizational_Performance_in_a_Sudanese_University">Factors Associated with Occupational Stress and Their Effects on Organizational Performance in a Sudanese University</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Occupational stress has a significant impact on student learning and thereby on the contribution that such institutions can make to society. This affects organizational performance by reducing productivity and ef-ficiency which affect the... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_69861411" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Occupational stress has a significant impact on student learning and thereby on the contribution that such institutions can make to society. This affects organizational performance by reducing productivity and ef-ficiency which affect the organization negatively. The aim of the current study was to determine the fac-tors associated with occupational stress and their relationship with organizational performance at one of the private universities in Sudan. A total of 150 male and female employees from different departments and with various educational levels in the main building of the university were randomly selected. Data was collected using a questionnaire with background questions, job stressors such as role conflict and ambiguity, lack of participation in decision making, lack of authority, workload, unsatisfactory working conditions and interpersonal relationships, and statements about the effect on organisational performance. Questions were based on three- and four-point scale...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/69861411" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="47684ba5b87e5cb767cce2599fedd4a4" rel="nofollow" data-download="{"attachment_id":79797127,"asset_id":69861411,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/79797127/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="182241663" href="https://taibahu.academia.edu/AElshikieri">Ahlam El shikieri</a><script data-card-contents-for-user="182241663" type="text/json">{"id":182241663,"first_name":"Ahlam","last_name":"El shikieri","domain_name":"taibahu","page_name":"AElshikieri","display_name":"Ahlam El shikieri","profile_url":"https://taibahu.academia.edu/AElshikieri?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_69861411 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="69861411"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 69861411, container: ".js-paper-rank-work_69861411", }); });</script></li><li class="js-percentile-work_69861411 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 69861411; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_69861411"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_69861411 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="69861411"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 69861411; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=69861411]").text(description); $(".js-view-count-work_69861411").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_69861411").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="69861411"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">8</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="922" rel="nofollow" href="https://www.academia.edu/Documents/in/Education">Education</a>, <script data-card-contents-for-ri="922" type="text/json">{"id":922,"name":"Education","url":"https://www.academia.edu/Documents/in/Education?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="2621" rel="nofollow" href="https://www.academia.edu/Documents/in/Higher_Education">Higher Education</a>, <script data-card-contents-for-ri="2621" type="text/json">{"id":2621,"name":"Higher Education","url":"https://www.academia.edu/Documents/in/Higher_Education?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="26327" rel="nofollow" href="https://www.academia.edu/Documents/in/Medicine">Medicine</a><script data-card-contents-for-ri="26327" type="text/json">{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=69861411]'), work: {"id":69861411,"title":"Factors Associated with Occupational Stress and Their Effects on Organizational Performance in a Sudanese University","created_at":"2022-01-28T23:06:22.083-08:00","url":"https://www.academia.edu/69861411/Factors_Associated_with_Occupational_Stress_and_Their_Effects_on_Organizational_Performance_in_a_Sudanese_University?f_ri=19156","dom_id":"work_69861411","summary":"Occupational stress has a significant impact on student learning and thereby on the contribution that such institutions can make to society. This affects organizational performance by reducing productivity and ef-ficiency which affect the organization negatively. The aim of the current study was to determine the fac-tors associated with occupational stress and their relationship with organizational performance at one of the private universities in Sudan. A total of 150 male and female employees from different departments and with various educational levels in the main building of the university were randomly selected. Data was collected using a questionnaire with background questions, job stressors such as role conflict and ambiguity, lack of participation in decision making, lack of authority, workload, unsatisfactory working conditions and interpersonal relationships, and statements about the effect on organisational performance. Questions were based on three- and four-point scale...","downloadable_attachments":[{"id":79797127,"asset_id":69861411,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":182241663,"first_name":"Ahlam","last_name":"El shikieri","domain_name":"taibahu","page_name":"AElshikieri","display_name":"Ahlam El shikieri","profile_url":"https://taibahu.academia.edu/AElshikieri?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":922,"name":"Education","url":"https://www.academia.edu/Documents/in/Education?f_ri=19156","nofollow":true},{"id":2621,"name":"Higher Education","url":"https://www.academia.edu/Documents/in/Higher_Education?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine?f_ri=19156","nofollow":true},{"id":32572,"name":"Sudan","url":"https://www.academia.edu/Documents/in/Sudan?f_ri=19156"},{"id":117208,"name":"Organizational Performance","url":"https://www.academia.edu/Documents/in/Organizational_Performance?f_ri=19156"},{"id":117714,"name":"Creative Education","url":"https://www.academia.edu/Documents/in/Creative_Education?f_ri=19156"},{"id":559138,"name":"Occupational Stress","url":"https://www.academia.edu/Documents/in/Occupational_Stress?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_55339224" data-work_id="55339224" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/55339224/Mercury_and_Alzheimers_Disease_HG_II_Ions_Display_Specific_Binding_to_the_Amyloid_Beta_Peptide_and_Modulate_its_Aggregation">Mercury and Alzheimers Disease: HG(II) Ions Display Specific Binding to the Amyloid-Beta Peptide and Modulate its Aggregation</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Brains and blood of Alzheimer's disease (AD) patients have shown elevated mercury concentrations, but potential involvement of mercury exposure in AD pathogenesis has not been studied at the molecular level. The pathological hallmark of... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_55339224" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Brains and blood of Alzheimer's disease (AD) patients have shown elevated mercury concentrations, but potential involvement of mercury exposure in AD pathogenesis has not been studied at the molecular level. The pathological hallmark of AD brains is deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils. Aβ peptide fibrillization is known to be modulated by metal ions such as Cu(II) and Zn(II). Here, we study in vitro the interactions between Aβ peptides and Hg(II) ions by multiple biophysical techniques. Fluorescence spectroscopy and atomic force microscopy (AFM) show that Hg(II) ions have a concentration-dependent inhibiting effect on Aβ fibrillization: at a 1:1 Aβ•Hg(II) ratio only non-fibrillar Aβ aggregates are formed. NMR spectroscopy shows that Hg(II) ions interact with the N-terminal region of Aβ(1-40) with a micromolar affinity, likely via a binding mode similar to that for Cu(II) and Zn(II) ions, i.e., mainly via the histidine residues His6, His13, and His14. Thus, together with Cu(II), Fe(II), Mn(II), Pb(IV), and Zn(II) ions, Hg(II) belongs to a family of metal ions that display residue-specific binding interactions with Aβ peptides and modulate their aggregation processes.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/55339224" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="c063104a7b5e3fcd51e2e6f967f509bd" rel="nofollow" data-download="{"attachment_id":71255379,"asset_id":55339224,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/71255379/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33838722" href="https://ttu-ee.academia.edu/PeepPalumaa">Peep Palumaa</a><script data-card-contents-for-user="33838722" type="text/json">{"id":33838722,"first_name":"Peep","last_name":"Palumaa","domain_name":"ttu-ee","page_name":"PeepPalumaa","display_name":"Peep Palumaa","profile_url":"https://ttu-ee.academia.edu/PeepPalumaa?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_55339224 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="55339224"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 55339224, container: ".js-paper-rank-work_55339224", }); 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$(".js-view-count[data-work-id=55339224]").text(description); $(".js-view-count-work_55339224").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_55339224").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="55339224"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">5</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a>, <script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="260118" rel="nofollow" href="https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES">CHEMICAL SCIENCES</a><script data-card-contents-for-ri="260118" type="text/json">{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=55339224]'), work: {"id":55339224,"title":"Mercury and Alzheimers Disease: HG(II) Ions Display Specific Binding to the Amyloid-Beta Peptide and Modulate its Aggregation","created_at":"2021-10-04T00:09:00.077-07:00","url":"https://www.academia.edu/55339224/Mercury_and_Alzheimers_Disease_HG_II_Ions_Display_Specific_Binding_to_the_Amyloid_Beta_Peptide_and_Modulate_its_Aggregation?f_ri=19156","dom_id":"work_55339224","summary":"Brains and blood of Alzheimer's disease (AD) patients have shown elevated mercury concentrations, but potential involvement of mercury exposure in AD pathogenesis has not been studied at the molecular level. The pathological hallmark of AD brains is deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils. Aβ peptide fibrillization is known to be modulated by metal ions such as Cu(II) and Zn(II). Here, we study in vitro the interactions between Aβ peptides and Hg(II) ions by multiple biophysical techniques. Fluorescence spectroscopy and atomic force microscopy (AFM) show that Hg(II) ions have a concentration-dependent inhibiting effect on Aβ fibrillization: at a 1:1 Aβ•Hg(II) ratio only non-fibrillar Aβ aggregates are formed. NMR spectroscopy shows that Hg(II) ions interact with the N-terminal region of Aβ(1-40) with a micromolar affinity, likely via a binding mode similar to that for Cu(II) and Zn(II) ions, i.e., mainly via the histidine residues His6, His13, and His14. Thus, together with Cu(II), Fe(II), Mn(II), Pb(IV), and Zn(II) ions, Hg(II) belongs to a family of metal ions that display residue-specific binding interactions with Aβ peptides and modulate their aggregation processes.","downloadable_attachments":[{"id":71255379,"asset_id":55339224,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33838722,"first_name":"Peep","last_name":"Palumaa","domain_name":"ttu-ee","page_name":"PeepPalumaa","display_name":"Peep Palumaa","profile_url":"https://ttu-ee.academia.edu/PeepPalumaa?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true},{"id":402990,"name":"Biomolecules","url":"https://www.academia.edu/Documents/in/Biomolecules?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_54616488" data-work_id="54616488" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/54616488/HIV_1_Capsid_Protein_Forms_Spherical_Immature_Like_and_Tubular_Mature_Like_Particles_in_Vitro_Structure_Switching_by_pH_induced_Conformational_Changes">HIV-1 Capsid Protein Forms Spherical (Immature-Like) and Tubular (Mature-Like) Particles in Vitro: Structure Switching by pH-induced Conformational Changes</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The viral genome and replicative enzymes of the human immunodeficiency virus are encased in a shell consisting of assembled mature capsid protein (CA). The core shell is a stable, effective protective barrier, but is also poised for... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_54616488" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The viral genome and replicative enzymes of the human immunodeficiency virus are encased in a shell consisting of assembled mature capsid protein (CA). The core shell is a stable, effective protective barrier, but is also poised for dissolution on cue to allow transmission of the viral genome into its new host. In this study, static light scattering (SLS) and dynamic light scattering (DLS) were used to examine the entire range of the CA protein response to an environmental cue (pH). The CA protein assembled tubular structures as previously reported but also was capable of assembling spheres, depending on the pH of the protein solution. The switch from formation of one to the other occurred within a very narrow physiological pH range (i.e., pH 7.0 to pH 6.8). Below this range, only dimers were detected. Above this range, the previously described tubular structures were detected. The ability of the CA protein to form a spherical structure that is detectable by DLS but not by electron microscopy indicates that some assemblages are inherently sensitive to perturbation. The dimers in equilibrium with these assemblages exhibited distinct conformations: Dimers in equilibrium with the spherical form exhibited a compact conformation. Dimers in equilibrium with the rod-like form had an extended conformation. Thus, the CA protein possesses the inherent ability to form metastable structures, the morphology of which is regulated by an environmentallysensitive molecular switch. Such metastable structures may exist as transient intermediates during the assembly and/or disassembly of the virus core.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/54616488" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="fd7460ca0d5ce3da2629d4735313b9fe" rel="nofollow" data-download="{"attachment_id":70896409,"asset_id":54616488,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/70896409/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="53799628" href="https://independent.academia.edu/BenjaminChu1">Benjamin Chu</a><script data-card-contents-for-user="53799628" type="text/json">{"id":53799628,"first_name":"Benjamin","last_name":"Chu","domain_name":"independent","page_name":"BenjaminChu1","display_name":"Benjamin Chu","profile_url":"https://independent.academia.edu/BenjaminChu1?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_54616488 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="54616488"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 54616488, container: ".js-paper-rank-work_54616488", }); });</script></li><li class="js-percentile-work_54616488 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 54616488; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_54616488"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_54616488 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="54616488"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 54616488; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=54616488]").text(description); $(".js-view-count-work_54616488").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_54616488").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="54616488"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">19</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="2184" rel="nofollow" href="https://www.academia.edu/Documents/in/Electron_Microscopy">Electron Microscopy</a>, <script data-card-contents-for-ri="2184" type="text/json">{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="39978" rel="nofollow" href="https://www.academia.edu/Documents/in/HIV">HIV</a>, <script data-card-contents-for-ri="39978" type="text/json">{"id":39978,"name":"HIV","url":"https://www.academia.edu/Documents/in/HIV?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a><script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=54616488]'), work: {"id":54616488,"title":"HIV-1 Capsid Protein Forms Spherical (Immature-Like) and Tubular (Mature-Like) Particles in Vitro: Structure Switching by pH-induced Conformational Changes","created_at":"2021-10-01T07:25:49.966-07:00","url":"https://www.academia.edu/54616488/HIV_1_Capsid_Protein_Forms_Spherical_Immature_Like_and_Tubular_Mature_Like_Particles_in_Vitro_Structure_Switching_by_pH_induced_Conformational_Changes?f_ri=19156","dom_id":"work_54616488","summary":"The viral genome and replicative enzymes of the human immunodeficiency virus are encased in a shell consisting of assembled mature capsid protein (CA). The core shell is a stable, effective protective barrier, but is also poised for dissolution on cue to allow transmission of the viral genome into its new host. In this study, static light scattering (SLS) and dynamic light scattering (DLS) were used to examine the entire range of the CA protein response to an environmental cue (pH). The CA protein assembled tubular structures as previously reported but also was capable of assembling spheres, depending on the pH of the protein solution. The switch from formation of one to the other occurred within a very narrow physiological pH range (i.e., pH 7.0 to pH 6.8). Below this range, only dimers were detected. Above this range, the previously described tubular structures were detected. The ability of the CA protein to form a spherical structure that is detectable by DLS but not by electron microscopy indicates that some assemblages are inherently sensitive to perturbation. The dimers in equilibrium with these assemblages exhibited distinct conformations: Dimers in equilibrium with the spherical form exhibited a compact conformation. Dimers in equilibrium with the rod-like form had an extended conformation. Thus, the CA protein possesses the inherent ability to form metastable structures, the morphology of which is regulated by an environmentallysensitive molecular switch. Such metastable structures may exist as transient intermediates during the assembly and/or disassembly of the virus core.","downloadable_attachments":[{"id":70896409,"asset_id":54616488,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":53799628,"first_name":"Benjamin","last_name":"Chu","domain_name":"independent","page_name":"BenjaminChu1","display_name":"Benjamin Chu","profile_url":"https://independent.academia.edu/BenjaminChu1?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":39978,"name":"HIV","url":"https://www.academia.edu/Documents/in/HIV?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":128057,"name":"Light","url":"https://www.academia.edu/Documents/in/Light?f_ri=19156"},{"id":142451,"name":"Dynamic Light Scattering","url":"https://www.academia.edu/Documents/in/Dynamic_Light_Scattering?f_ri=19156"},{"id":201140,"name":"Capsid","url":"https://www.academia.edu/Documents/in/Capsid?f_ri=19156"},{"id":231661,"name":"Enzyme","url":"https://www.academia.edu/Documents/in/Enzyme?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":318308,"name":"Human immunodeficiency virus","url":"https://www.academia.edu/Documents/in/Human_immunodeficiency_virus?f_ri=19156"},{"id":414692,"name":"Solutions","url":"https://www.academia.edu/Documents/in/Solutions?f_ri=19156"},{"id":695018,"name":"Molecular weight","url":"https://www.academia.edu/Documents/in/Molecular_weight?f_ri=19156"},{"id":956752,"name":"Protein Quaternary Structure","url":"https://www.academia.edu/Documents/in/Protein_Quaternary_Structure?f_ri=19156"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=19156"},{"id":1248637,"name":"Capsid Protein","url":"https://www.academia.edu/Documents/in/Capsid_Protein?f_ri=19156"},{"id":1274450,"name":"Conformational Change","url":"https://www.academia.edu/Documents/in/Conformational_Change?f_ri=19156"},{"id":1809037,"name":"Dimerization","url":"https://www.academia.edu/Documents/in/Dimerization?f_ri=19156"},{"id":2482932,"name":"Pliability","url":"https://www.academia.edu/Documents/in/Pliability?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_30633031" data-work_id="30633031" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/30633031/Ligand_exchange_effects_in_gold_nanoparticle_assembly_induced_by_oxidative_stress_biomarkers_Homocysteine_and_cysteine">Ligand exchange effects in gold nanoparticle assembly induced by oxidative stress biomarkers: Homocysteine and cysteine</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The interactions of oxidative stress biomarkers: homocysteine (Hcys) and cysteine (Cys) with the multifunctional gold nanoparticles, important in view of novel biomedical applications in diagnostics and therapy, have been investigated... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_30633031" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The interactions of oxidative stress biomarkers: homocysteine (Hcys) and cysteine (Cys) with the multifunctional gold nanoparticles, important in view of novel biomedical applications in diagnostics and therapy, have been investigated using resonance elastic light scattering (RELS), UV-Vis plasmonic spectroscopy, and high-resolution TEM imaging. The Hcys-induced assembly of gold nanoparticles has been observed for non-ionic surfactant-capped gold nanoparticles as well as for negatively-charged citrate-capped gold nanoparticles. We have observed for the first time the de-aggregation of citrate-capped gold nanoparticle ensembles followed by their conversion to citrate-linked Hcys-capped nanoparticle assemblies. The Cys molecules, which are smaller than Hcys by only one CH(2) group, show much less activity. The mechanisms leading to this intriguing disparity in the abilities of these two thioaminoacids to ligand exchange with surfactant- or citrate-capping molecules of the gold nanoparticle shells are proposed on the basis of the experimental evidence, molecular dynamics simulations, and quantum mechanical calculations. For citrate-capped gold nanoparticles, we postulate the formation of surface complexes facilitated by electrostatic attractions and formation of double hydrogen bonds for both Hcys and Cys. The conformational differences between these two kinds of complexes result in marked differences in the distance between -SH groups of the biomarkers to the gold surface and different abilities to induce nanoparticle assembly. Analytical implications of these mechanistic differences are discussed.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/30633031" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="7f0800a713792514bab578c3bdfc688e" rel="nofollow" data-download="{"attachment_id":51166966,"asset_id":30633031,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/51166966/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="58288344" href="https://potsdam.academia.edu/MariaHepel">Maria R Hepel</a><script data-card-contents-for-user="58288344" type="text/json">{"id":58288344,"first_name":"Maria","last_name":"Hepel","domain_name":"potsdam","page_name":"MariaHepel","display_name":"Maria R Hepel","profile_url":"https://potsdam.academia.edu/MariaHepel?f_ri=19156","photo":"https://0.academia-photos.com/58288344/25560145/24275668/s65_maria.hepel.jpg"}</script></span></span></li><li class="js-paper-rank-work_30633031 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="30633031"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 30633031, container: ".js-paper-rank-work_30633031", }); });</script></li><li class="js-percentile-work_30633031 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 30633031; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_30633031"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_30633031 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="30633031"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 30633031; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=30633031]").text(description); $(".js-view-count-work_30633031").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_30633031").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="30633031"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">19</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="2736" rel="nofollow" href="https://www.academia.edu/Documents/in/Molecular_Dynamics_Simulation">Molecular Dynamics Simulation</a>, <script data-card-contents-for-ri="2736" type="text/json">{"id":2736,"name":"Molecular Dynamics Simulation","url":"https://www.academia.edu/Documents/in/Molecular_Dynamics_Simulation?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="4512" rel="nofollow" href="https://www.academia.edu/Documents/in/Light_Scattering">Light Scattering</a>, <script data-card-contents-for-ri="4512" type="text/json">{"id":4512,"name":"Light Scattering","url":"https://www.academia.edu/Documents/in/Light_Scattering?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="14292" rel="nofollow" href="https://www.academia.edu/Documents/in/Oxidative_Stress">Oxidative Stress</a>, <script data-card-contents-for-ri="14292" type="text/json">{"id":14292,"name":"Oxidative Stress","url":"https://www.academia.edu/Documents/in/Oxidative_Stress?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a><script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=30633031]'), work: {"id":30633031,"title":"Ligand exchange effects in gold nanoparticle assembly induced by oxidative stress biomarkers: Homocysteine and cysteine","created_at":"2016-12-27T07:42:29.137-08:00","url":"https://www.academia.edu/30633031/Ligand_exchange_effects_in_gold_nanoparticle_assembly_induced_by_oxidative_stress_biomarkers_Homocysteine_and_cysteine?f_ri=19156","dom_id":"work_30633031","summary":"The interactions of oxidative stress biomarkers: homocysteine (Hcys) and cysteine (Cys) with the multifunctional gold nanoparticles, important in view of novel biomedical applications in diagnostics and therapy, have been investigated using resonance elastic light scattering (RELS), UV-Vis plasmonic spectroscopy, and high-resolution TEM imaging. The Hcys-induced assembly of gold nanoparticles has been observed for non-ionic surfactant-capped gold nanoparticles as well as for negatively-charged citrate-capped gold nanoparticles. We have observed for the first time the de-aggregation of citrate-capped gold nanoparticle ensembles followed by their conversion to citrate-linked Hcys-capped nanoparticle assemblies. The Cys molecules, which are smaller than Hcys by only one CH(2) group, show much less activity. The mechanisms leading to this intriguing disparity in the abilities of these two thioaminoacids to ligand exchange with surfactant- or citrate-capping molecules of the gold nanoparticle shells are proposed on the basis of the experimental evidence, molecular dynamics simulations, and quantum mechanical calculations. For citrate-capped gold nanoparticles, we postulate the formation of surface complexes facilitated by electrostatic attractions and formation of double hydrogen bonds for both Hcys and Cys. The conformational differences between these two kinds of complexes result in marked differences in the distance between -SH groups of the biomarkers to the gold surface and different abilities to induce nanoparticle assembly. Analytical implications of these mechanistic differences are discussed.","downloadable_attachments":[{"id":51166966,"asset_id":30633031,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":58288344,"first_name":"Maria","last_name":"Hepel","domain_name":"potsdam","page_name":"MariaHepel","display_name":"Maria R Hepel","profile_url":"https://potsdam.academia.edu/MariaHepel?f_ri=19156","photo":"https://0.academia-photos.com/58288344/25560145/24275668/s65_maria.hepel.jpg"}],"research_interests":[{"id":2736,"name":"Molecular Dynamics Simulation","url":"https://www.academia.edu/Documents/in/Molecular_Dynamics_Simulation?f_ri=19156","nofollow":true},{"id":4512,"name":"Light Scattering","url":"https://www.academia.edu/Documents/in/Light_Scattering?f_ri=19156","nofollow":true},{"id":14292,"name":"Oxidative Stress","url":"https://www.academia.edu/Documents/in/Oxidative_Stress?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":35056,"name":"Metal Nanoparticles","url":"https://www.academia.edu/Documents/in/Metal_Nanoparticles?f_ri=19156"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":65698,"name":"Gold nanoparticle","url":"https://www.academia.edu/Documents/in/Gold_nanoparticle?f_ri=19156"},{"id":76736,"name":"Gold","url":"https://www.academia.edu/Documents/in/Gold?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":128057,"name":"Light","url":"https://www.academia.edu/Documents/in/Light?f_ri=19156"},{"id":195983,"name":"Homocysteine","url":"https://www.academia.edu/Documents/in/Homocysteine?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":413195,"name":"Time Factors","url":"https://www.academia.edu/Documents/in/Time_Factors?f_ri=19156"},{"id":444844,"name":"Spectrum analysis","url":"https://www.academia.edu/Documents/in/Spectrum_analysis?f_ri=19156"},{"id":568482,"name":"Biological markers","url":"https://www.academia.edu/Documents/in/Biological_markers?f_ri=19156"},{"id":614749,"name":"Cysteine","url":"https://www.academia.edu/Documents/in/Cysteine?f_ri=19156"},{"id":649537,"name":"Molecular Conformation","url":"https://www.academia.edu/Documents/in/Molecular_Conformation?f_ri=19156"},{"id":1222191,"name":"Ligands","url":"https://www.academia.edu/Documents/in/Ligands?f_ri=19156"},{"id":1297608,"name":"Organic Chemicals","url":"https://www.academia.edu/Documents/in/Organic_Chemicals?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_2244842" data-work_id="2244842" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/2244842/Laccases_stabilization_with_phosphatidylcholine_liposomes">Laccases stabilization with phosphatidylcholine liposomes</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">In recent years, there has been an upsurge of interest in enzyme treatment of textile fibres. Enzymes are globular proteins whose catalytic function is due to their three dimensional structure. For this reason, stability strategies make... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_2244842" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">In recent years, there has been an upsurge of interest in enzyme treatment of textile fibres. Enzymes are globular proteins whose catalytic function is due to their three dimensional structure. For this reason, stability strategies make use of compounds that avoid dismantling or distorting protein 3D structures. This study is concerned with the use of microencapsulation techniques to optimize enzyme stabilization. Laccases were embedded in phophatidylcholine liposomes and their encapsulation capacity was assessed. Their enzymatic activity and stability were analyzed, comparing free-enzymes, enzymes in liposomes, and the lipid fraction separated from the aqueous fraction. An increase in their encapsulation efficiency was found at higher lipid/laccase ratios. Relative activity of enzyme-containing vesicles has also been shown to be retained much more than that of free native enzymes. The loss of activity of laccases entrapped in the vesicles in the total stability process is lower than 10% compared with 40% to 60% of loss of free-laccases after heating the samples for 3 days. Laccase stabilization could be of interest to future textile or cosmetic applications because of their potential for environmentally friendly oxidation technologies.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/2244842" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="6c03ef2d1b7fb4aa5fdc2809cc54e1b8" rel="nofollow" data-download="{"attachment_id":30296419,"asset_id":2244842,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/30296419/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="1886010" href="https://uminho.academia.edu/AndreaZille">Andrea Zille</a><script data-card-contents-for-user="1886010" type="text/json">{"id":1886010,"first_name":"Andrea","last_name":"Zille","domain_name":"uminho","page_name":"AndreaZille","display_name":"Andrea Zille","profile_url":"https://uminho.academia.edu/AndreaZille?f_ri=19156","photo":"https://0.academia-photos.com/1886010/866708/1081453/s65_andrea.zille.jpg"}</script></span></span></li><li class="js-paper-rank-work_2244842 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="2244842"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 2244842, container: ".js-paper-rank-work_2244842", }); });</script></li><li class="js-percentile-work_2244842 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 2244842; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_2244842"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_2244842 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="2244842"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 2244842; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=2244842]").text(description); $(".js-view-count-work_2244842").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_2244842").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="2244842"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">4</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="25600" rel="nofollow" href="https://www.academia.edu/Documents/in/Stability">Stability</a>, <script data-card-contents-for-ri="25600" type="text/json">{"id":25600,"name":"Stability","url":"https://www.academia.edu/Documents/in/Stability?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="286636" rel="nofollow" href="https://www.academia.edu/Documents/in/Encapsulation">Encapsulation</a>, <script data-card-contents-for-ri="286636" type="text/json">{"id":286636,"name":"Encapsulation","url":"https://www.academia.edu/Documents/in/Encapsulation?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="386603" rel="nofollow" href="https://www.academia.edu/Documents/in/LACCASES">LACCASES</a><script data-card-contents-for-ri="386603" type="text/json">{"id":386603,"name":"LACCASES","url":"https://www.academia.edu/Documents/in/LACCASES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=2244842]'), work: {"id":2244842,"title":"Laccases stabilization with phosphatidylcholine liposomes","created_at":"2012-12-05T18:22:23.729-08:00","url":"https://www.academia.edu/2244842/Laccases_stabilization_with_phosphatidylcholine_liposomes?f_ri=19156","dom_id":"work_2244842","summary":"In recent years, there has been an upsurge of interest in enzyme treatment of textile fibres. Enzymes are globular proteins whose catalytic function is due to their three dimensional structure. For this reason, stability strategies make use of compounds that avoid dismantling or distorting protein 3D structures. This study is concerned with the use of microencapsulation techniques to optimize enzyme stabilization. Laccases were embedded in phophatidylcholine liposomes and their encapsulation capacity was assessed. Their enzymatic activity and stability were analyzed, comparing free-enzymes, enzymes in liposomes, and the lipid fraction separated from the aqueous fraction. An increase in their encapsulation efficiency was found at higher lipid/laccase ratios. Relative activity of enzyme-containing vesicles has also been shown to be retained much more than that of free native enzymes. The loss of activity of laccases entrapped in the vesicles in the total stability process is lower than 10% compared with 40% to 60% of loss of free-laccases after heating the samples for 3 days. Laccase stabilization could be of interest to future textile or cosmetic applications because of their potential for environmentally friendly oxidation technologies.","downloadable_attachments":[{"id":30296419,"asset_id":2244842,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":1886010,"first_name":"Andrea","last_name":"Zille","domain_name":"uminho","page_name":"AndreaZille","display_name":"Andrea Zille","profile_url":"https://uminho.academia.edu/AndreaZille?f_ri=19156","photo":"https://0.academia-photos.com/1886010/866708/1081453/s65_andrea.zille.jpg"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":25600,"name":"Stability","url":"https://www.academia.edu/Documents/in/Stability?f_ri=19156","nofollow":true},{"id":286636,"name":"Encapsulation","url":"https://www.academia.edu/Documents/in/Encapsulation?f_ri=19156","nofollow":true},{"id":386603,"name":"LACCASES","url":"https://www.academia.edu/Documents/in/LACCASES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_10825734" data-work_id="10825734" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/10825734/Decoding_of_Calcium_Oscillations_by_Phosphorylation_Cycles_Analytic_Results">Decoding of Calcium Oscillations by Phosphorylation Cycles: Analytic Results</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Experimental studies have demonstrated that Ca 21 -regulated proteins are sensitive to the frequency of Ca 21 oscillations, and several mathematical models for specific proteins have provided insight into the mechanisms involved. Because... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_10825734" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Experimental studies have demonstrated that Ca 21 -regulated proteins are sensitive to the frequency of Ca 21 oscillations, and several mathematical models for specific proteins have provided insight into the mechanisms involved. Because of the large number of Ca 21 -regulated proteins in signal transduction, metabolism and gene expression, it is desirable to establish in general terms which molecular properties shape the response to oscillatory Ca 21 signals. Here we address this question by analyzing in detail a model of a prototypical Ca 21 -decoding module, consisting of a target protein whose activity is controlled by a Ca 21 -activated kinase and the counteracting phosphatase. We show that this module can decode the frequency of Ca 21 oscillations, at constant average Ca 21 signal, provided that the Ca 21 spikes are narrow and the oscillation frequency is sufficiently low-of the order of the phosphatase rate constant or below. Moreover, Ca 21 oscillations activate the target more efficiently than a constant signal when Ca 21 is bound cooperatively and with low affinity. Thus, the rate constants and the Ca 21 affinities of the target-modifying enzymes can be tuned in such a way that the module responds optimally to Ca 21 spikes of a certain amplitude and frequency. Frequency sensitivity is further enhanced when the limited duration of the external stimulus driving Ca 21 signaling is accounted for. Thus, our study identifies molecular parameters that may be involved in establishing the specificity of cellular responses downstream of Ca 21 oscillations.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/10825734" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="b112f2c8f09f50bfcc7b1647dabfbdb7" rel="nofollow" data-download="{"attachment_id":47095331,"asset_id":10825734,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/47095331/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="26317598" href="https://independent.academia.edu/CarlosSalazar50">Carlos Salazar</a><script data-card-contents-for-user="26317598" type="text/json">{"id":26317598,"first_name":"Carlos","last_name":"Salazar","domain_name":"independent","page_name":"CarlosSalazar50","display_name":"Carlos Salazar","profile_url":"https://independent.academia.edu/CarlosSalazar50?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_10825734 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="10825734"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 10825734, container: ".js-paper-rank-work_10825734", }); });</script></li><li class="js-percentile-work_10825734 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 10825734; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_10825734"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_10825734 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="10825734"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 10825734; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=10825734]").text(description); $(".js-view-count-work_10825734").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_10825734").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="10825734"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">15</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="27784" rel="nofollow" href="https://www.academia.edu/Documents/in/Gene_expression">Gene expression</a>, <script data-card-contents-for-ri="27784" type="text/json">{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="38831" rel="nofollow" href="https://www.academia.edu/Documents/in/Signal_Transduction">Signal Transduction</a><script data-card-contents-for-ri="38831" type="text/json">{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=10825734]'), work: {"id":10825734,"title":"Decoding of Calcium Oscillations by Phosphorylation Cycles: Analytic Results","created_at":"2015-02-15T21:06:23.764-08:00","url":"https://www.academia.edu/10825734/Decoding_of_Calcium_Oscillations_by_Phosphorylation_Cycles_Analytic_Results?f_ri=19156","dom_id":"work_10825734","summary":"Experimental studies have demonstrated that Ca 21 -regulated proteins are sensitive to the frequency of Ca 21 oscillations, and several mathematical models for specific proteins have provided insight into the mechanisms involved. Because of the large number of Ca 21 -regulated proteins in signal transduction, metabolism and gene expression, it is desirable to establish in general terms which molecular properties shape the response to oscillatory Ca 21 signals. Here we address this question by analyzing in detail a model of a prototypical Ca 21 -decoding module, consisting of a target protein whose activity is controlled by a Ca 21 -activated kinase and the counteracting phosphatase. We show that this module can decode the frequency of Ca 21 oscillations, at constant average Ca 21 signal, provided that the Ca 21 spikes are narrow and the oscillation frequency is sufficiently low-of the order of the phosphatase rate constant or below. Moreover, Ca 21 oscillations activate the target more efficiently than a constant signal when Ca 21 is bound cooperatively and with low affinity. Thus, the rate constants and the Ca 21 affinities of the target-modifying enzymes can be tuned in such a way that the module responds optimally to Ca 21 spikes of a certain amplitude and frequency. Frequency sensitivity is further enhanced when the limited duration of the external stimulus driving Ca 21 signaling is accounted for. Thus, our study identifies molecular parameters that may be involved in establishing the specificity of cellular responses downstream of Ca 21 oscillations.","downloadable_attachments":[{"id":47095331,"asset_id":10825734,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":26317598,"first_name":"Carlos","last_name":"Salazar","domain_name":"independent","page_name":"CarlosSalazar50","display_name":"Carlos Salazar","profile_url":"https://independent.academia.edu/CarlosSalazar50?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=19156","nofollow":true},{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":69542,"name":"Computer Simulation","url":"https://www.academia.edu/Documents/in/Computer_Simulation?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":140081,"name":"Calcium Signaling","url":"https://www.academia.edu/Documents/in/Calcium_Signaling?f_ri=19156"},{"id":172083,"name":"Phosphorylation","url":"https://www.academia.edu/Documents/in/Phosphorylation?f_ri=19156"},{"id":174781,"name":"Oscillations","url":"https://www.academia.edu/Documents/in/Oscillations?f_ri=19156"},{"id":215075,"name":"Experimental Study","url":"https://www.academia.edu/Documents/in/Experimental_Study?f_ri=19156"},{"id":231661,"name":"Enzyme","url":"https://www.academia.edu/Documents/in/Enzyme?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":291387,"name":"Mathematical Model","url":"https://www.academia.edu/Documents/in/Mathematical_Model?f_ri=19156"},{"id":842314,"name":"Biological clocks","url":"https://www.academia.edu/Documents/in/Biological_clocks?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_14228919" data-work_id="14228919" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/14228919/Variance_analysis_of_gamma_aminobutyric_acid_GABA_ergic_inhibitory_postsynaptic_currents_from_melanotropes_of_Xenopus_laevis">Variance analysis of gamma-aminobutyric acid (GABA)-ergic inhibitory postsynaptic currents from melanotropes of Xenopus laevis</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">We have studied the variance in the decay of large spontaneous y-aminobutyric acid (GABA)-ergic inhibitory postsynaptic currents (IPSCs) in melanotropes of Xenopus laevis to obtain information about the number of GABAA receptor channels... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_14228919" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">We have studied the variance in the decay of large spontaneous y-aminobutyric acid (GABA)-ergic inhibitory postsynaptic currents (IPSCs) in melanotropes of Xenopus laevis to obtain information about the number of GABAA receptor channels that bind GABA during the IPSCs. The average decay of the IPSCs is well described by the sum of two exponential functions. This suggests that a three-state Markov model is sufficient to describe the decay phase, with one of the three states being an absorbing state, entered when GABA dissociates from the GABAA receptor. We have compared the variance in the decay of large spontaneous IPSCs with the variance calculated for two different three-state models: a model with one open state, one closed state, and one absorbing state (1), and a model with two open states and one absorbing state (11). The data were better described by the more efficient model 11. This suggests that the efficacy of GABA at synaptic GABAA receptor channels is high and that only a small number of channels are involved in generating the GABA-ergic IPSCs.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/14228919" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="91a8fcbcd79a402783ecbe44bdcf3ef0" rel="nofollow" data-download="{"attachment_id":44432585,"asset_id":14228919,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/44432585/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33085165" href="https://ecu.academia.edu/MartinBier">Martin Bier</a><script data-card-contents-for-user="33085165" type="text/json">{"id":33085165,"first_name":"Martin","last_name":"Bier","domain_name":"ecu","page_name":"MartinBier","display_name":"Martin Bier","profile_url":"https://ecu.academia.edu/MartinBier?f_ri=19156","photo":"https://gravatar.com/avatar/fc693611b850df55d56750dce4a438ab?s=65"}</script></span></span></li><li class="js-paper-rank-work_14228919 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="14228919"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 14228919, container: ".js-paper-rank-work_14228919", }); 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The average decay of the IPSCs is well described by the sum of two exponential functions. This suggests that a three-state Markov model is sufficient to describe the decay phase, with one of the three states being an absorbing state, entered when GABA dissociates from the GABAA receptor. We have compared the variance in the decay of large spontaneous IPSCs with the variance calculated for two different three-state models: a model with one open state, one closed state, and one absorbing state (1), and a model with two open states and one absorbing state (11). The data were better described by the more efficient model 11. This suggests that the efficacy of GABA at synaptic GABAA receptor channels is high and that only a small number of channels are involved in generating the GABA-ergic IPSCs.","downloadable_attachments":[{"id":44432585,"asset_id":14228919,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33085165,"first_name":"Martin","last_name":"Bier","domain_name":"ecu","page_name":"MartinBier","display_name":"Martin Bier","profile_url":"https://ecu.academia.edu/MartinBier?f_ri=19156","photo":"https://gravatar.com/avatar/fc693611b850df55d56750dce4a438ab?s=65"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true},{"id":477264,"name":"Xenopus laevis","url":"https://www.academia.edu/Documents/in/Xenopus_laevis?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_21711926 coauthored" data-work_id="21711926" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/21711926/Hydration_Dependence_of_Conformational_Dielectric_Relaxation_of_Lysozyme">Hydration Dependence of Conformational Dielectric Relaxation of Lysozyme</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Dielectric response of hen egg white lysozyme is measured in the far infrared (5-65 cm ÿ1 , 0.15-1.95 THz, 0.6-8.1 meV) as a function of hydration. The frequency range is associated with collective vibrational modes of protein tertiary... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_21711926" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Dielectric response of hen egg white lysozyme is measured in the far infrared (5-65 cm ÿ1 , 0.15-1.95 THz, 0.6-8.1 meV) as a function of hydration. The frequency range is associated with collective vibrational modes of protein tertiary structure. The observed frequency dependence of the absorbance is broad and glass-like. For the entire frequency range, there is a slight increase in both the absorbance and index of refraction with increasing hydration for ,0.27 h (mass of H 2 O per unit mass protein). At 0.27 h, the absorbance and index begin to increase more rapidly. This transition corresponds to the point where the first hydration shell is filled. The abrupt increase in dielectric response cannot be fully accounted for by the additional contribution to the dielectric response due to bulk water, suggesting that the protein has not yet achieved its fully hydrated state. The broad, glass-like response suggests that at low hydrations, the low frequency conformational hen egg white lysozyme dynamics can be described by a dielectric relaxation model where the protein relaxes to different local minima in the conformational energy landscape. However, the low frequency complex permittivity does not allow for a pure relaxational mechanism. The data can best be modeled with a single low frequency resonance (n ; 120 GHz ¼ 4 cm ÿ1 ) and a single Debye relaxation process (t ; .03-.04 ps). Terahertz dielectric response is currently being considered as a possible biosensing technique and the results demonstrate the required hydration control necessary for reliable biosensor applications.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/21711926" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="9fa6bdd1c74f60065aff26ac78f057eb" rel="nofollow" data-download="{"attachment_id":42446210,"asset_id":21711926,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42446210/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="42991043" href="https://independent.academia.edu/JingYinChen">Jing-Yin Chen</a><script data-card-contents-for-user="42991043" type="text/json">{"id":42991043,"first_name":"Jing-Yin","last_name":"Chen","domain_name":"independent","page_name":"JingYinChen","display_name":"Jing-Yin Chen","profile_url":"https://independent.academia.edu/JingYinChen?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-21711926">+1</span><div class="hidden js-additional-users-21711926"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/AMarkelz">A. Markelz</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-21711926'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-21711926').html(); } } new HoverPopover(popoverSettings); })();</script></li><li class="js-paper-rank-work_21711926 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="21711926"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 21711926, container: ".js-paper-rank-work_21711926", }); });</script></li><li class="js-percentile-work_21711926 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 21711926; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_21711926"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_21711926 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="21711926"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 21711926; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=21711926]").text(description); $(".js-view-count-work_21711926").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_21711926").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="21711926"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">24</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="502" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysics">Biophysics</a>, <script data-card-contents-for-ri="502" type="text/json">{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="522" rel="nofollow" href="https://www.academia.edu/Documents/in/Thermodynamics">Thermodynamics</a>, <script data-card-contents-for-ri="522" type="text/json">{"id":522,"name":"Thermodynamics","url":"https://www.academia.edu/Documents/in/Thermodynamics?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="2215" rel="nofollow" href="https://www.academia.edu/Documents/in/Water">Water</a>, <script data-card-contents-for-ri="2215" type="text/json">{"id":2215,"name":"Water","url":"https://www.academia.edu/Documents/in/Water?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="4748" rel="nofollow" href="https://www.academia.edu/Documents/in/Electrochemistry">Electrochemistry</a><script data-card-contents-for-ri="4748" type="text/json">{"id":4748,"name":"Electrochemistry","url":"https://www.academia.edu/Documents/in/Electrochemistry?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=21711926]'), work: {"id":21711926,"title":"Hydration Dependence of Conformational Dielectric Relaxation of Lysozyme","created_at":"2016-02-08T21:06:17.050-08:00","url":"https://www.academia.edu/21711926/Hydration_Dependence_of_Conformational_Dielectric_Relaxation_of_Lysozyme?f_ri=19156","dom_id":"work_21711926","summary":"Dielectric response of hen egg white lysozyme is measured in the far infrared (5-65 cm ÿ1 , 0.15-1.95 THz, 0.6-8.1 meV) as a function of hydration. The frequency range is associated with collective vibrational modes of protein tertiary structure. The observed frequency dependence of the absorbance is broad and glass-like. For the entire frequency range, there is a slight increase in both the absorbance and index of refraction with increasing hydration for ,0.27 h (mass of H 2 O per unit mass protein). At 0.27 h, the absorbance and index begin to increase more rapidly. This transition corresponds to the point where the first hydration shell is filled. The abrupt increase in dielectric response cannot be fully accounted for by the additional contribution to the dielectric response due to bulk water, suggesting that the protein has not yet achieved its fully hydrated state. The broad, glass-like response suggests that at low hydrations, the low frequency conformational hen egg white lysozyme dynamics can be described by a dielectric relaxation model where the protein relaxes to different local minima in the conformational energy landscape. However, the low frequency complex permittivity does not allow for a pure relaxational mechanism. The data can best be modeled with a single low frequency resonance (n ; 120 GHz ¼ 4 cm ÿ1 ) and a single Debye relaxation process (t ; .03-.04 ps). Terahertz dielectric response is currently being considered as a possible biosensing technique and the results demonstrate the required hydration control necessary for reliable biosensor applications.","downloadable_attachments":[{"id":42446210,"asset_id":21711926,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":42991043,"first_name":"Jing-Yin","last_name":"Chen","domain_name":"independent","page_name":"JingYinChen","display_name":"Jing-Yin Chen","profile_url":"https://independent.academia.edu/JingYinChen?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":42897556,"first_name":"A.","last_name":"Markelz","domain_name":"independent","page_name":"AMarkelz","display_name":"A. Markelz","profile_url":"https://independent.academia.edu/AMarkelz?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":502,"name":"Biophysics","url":"https://www.academia.edu/Documents/in/Biophysics?f_ri=19156","nofollow":true},{"id":522,"name":"Thermodynamics","url":"https://www.academia.edu/Documents/in/Thermodynamics?f_ri=19156","nofollow":true},{"id":2215,"name":"Water","url":"https://www.academia.edu/Documents/in/Water?f_ri=19156","nofollow":true},{"id":4748,"name":"Electrochemistry","url":"https://www.academia.edu/Documents/in/Electrochemistry?f_ri=19156","nofollow":true},{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=19156"},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156"},{"id":30372,"name":"Low Frequency","url":"https://www.academia.edu/Documents/in/Low_Frequency?f_ri=19156"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156"},{"id":83315,"name":"Diffusion","url":"https://www.academia.edu/Documents/in/Diffusion?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":127997,"name":"Terahertz","url":"https://www.academia.edu/Documents/in/Terahertz?f_ri=19156"},{"id":181569,"name":"Proteins","url":"https://www.academia.edu/Documents/in/Proteins?f_ri=19156"},{"id":210279,"name":"Dielectric Relaxation","url":"https://www.academia.edu/Documents/in/Dielectric_Relaxation?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":318537,"name":"Local minima","url":"https://www.academia.edu/Documents/in/Local_minima?f_ri=19156"},{"id":335363,"name":"Far Infrared","url":"https://www.academia.edu/Documents/in/Far_Infrared?f_ri=19156"},{"id":349439,"name":"Frequency Dependence","url":"https://www.academia.edu/Documents/in/Frequency_Dependence?f_ri=19156"},{"id":402759,"name":"Chickens","url":"https://www.academia.edu/Documents/in/Chickens?f_ri=19156"},{"id":649537,"name":"Molecular Conformation","url":"https://www.academia.edu/Documents/in/Molecular_Conformation?f_ri=19156"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation?f_ri=19156"},{"id":749302,"name":"Indexation","url":"https://www.academia.edu/Documents/in/Indexation?f_ri=19156"},{"id":793580,"name":"Egg White","url":"https://www.academia.edu/Documents/in/Egg_White?f_ri=19156"},{"id":1412233,"name":"Biosensing Techniques","url":"https://www.academia.edu/Documents/in/Biosensing_Techniques?f_ri=19156"},{"id":1554801,"name":"Complex permittivity","url":"https://www.academia.edu/Documents/in/Complex_permittivity?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_77008593" data-work_id="77008593" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/77008593/Membrane_Interactions_in_Ionic_Solutions">Membrane Interactions in Ionic Solutions</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/77008593" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="22079b99c98c5b12b0910780fa6016d4" rel="nofollow" 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Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a><script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=77008593]'), work: {"id":77008593,"title":"Membrane Interactions in Ionic Solutions","created_at":"2022-04-19T18:15:52.988-07:00","url":"https://www.academia.edu/77008593/Membrane_Interactions_in_Ionic_Solutions?f_ri=19156","dom_id":"work_77008593","summary":null,"downloadable_attachments":[{"id":84537603,"asset_id":77008593,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":38257694,"first_name":"Bruce","last_name":"Ray","domain_name":"iu-indianapolis","page_name":"BRay","display_name":"Bruce D Ray","profile_url":"https://iu-indianapolis.academia.edu/BRay?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_7211286" data-work_id="7211286" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/7211286/Decrease_in_Size_of_Hen_Egg_white_Lysozyme_Aggregates_with_Decrease_in_Monomer_Concentration_from_Micro_to_Nanomolar_in_Alkaline_pH">Decrease in Size of Hen Egg white Lysozyme Aggregates with Decrease in Monomer Concentration from Micro to Nanomolar in Alkaline pH</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Protein aggregation leading to formation of amyloid fibrils is a symptom of several diseases like Alzheimer's, type 2 diabetes and so on. Elucidating the poorly understood mechanism of such phenomena entails the difficult task of... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_7211286" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Protein aggregation leading to formation of amyloid fibrils is a symptom of several diseases like Alzheimer's, type 2 diabetes and so on. Elucidating the poorly understood mechanism of such phenomena entails the difficult task of characterizing the species involved at each of the multiple steps in the aggregation pathway. It was previously shown by us that spontaneous aggregation of hen-eggwhite lysozyme (HEWL) at room temperature in pH 12.2 is a good model to study aggregation. Here in this paper we investigate the growth kinetics, structure, function and dynamics of multiple intermediate species populating the aggregation pathway of HEWL at pH 12.2. The different intermediates were isolated by varying the HEWL monomer concentration in the 300 nM-0.12 mM range. The intermediates were characterized using techniques like steady-state and nanosecond time-resolved fluorescence, atomic force microscopy and dynamic light scattering. Growth kinetics of non-fibrillar HEWL aggregates were fitted to the von Bertalanffy equation to yield a HEWL concentration independent rate constant (k = (6.660.6)610 25 s 21 ). Our results reveal stepwise changes in size, molecular packing and enzymatic activity among growing HEWL aggregates consistent with an isodesmic aggregation model. Formation of disulphide bonds that crosslink the monomers in the aggregate appear as a unique feature of this aggregation. AFM images of multiple amyloid fibrils emanating radially from amorphous aggregates directly confirmed that on-pathway fibril formation was feasible under isodesmic polymerization. The isolated HEWL aggregates are revealed as polycationic protein nanoparticles that are robust at neutral pH with ability to take up non-polar molecules like ANS.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/7211286" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="aa4acba9d98f649ce64dcdf5909dcc29" rel="nofollow" data-download="{"attachment_id":48561100,"asset_id":7211286,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/48561100/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="12516997" href="https://independent.academia.edu/AdityaIyer2">Aditya Iyer</a><script data-card-contents-for-user="12516997" type="text/json">{"id":12516997,"first_name":"Aditya","last_name":"Iyer","domain_name":"independent","page_name":"AdityaIyer2","display_name":"Aditya Iyer","profile_url":"https://independent.academia.edu/AdityaIyer2?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_7211286 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="7211286"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 7211286, container: ".js-paper-rank-work_7211286", }); 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Elucidating the poorly understood mechanism of such phenomena entails the difficult task of characterizing the species involved at each of the multiple steps in the aggregation pathway. It was previously shown by us that spontaneous aggregation of hen-eggwhite lysozyme (HEWL) at room temperature in pH 12.2 is a good model to study aggregation. Here in this paper we investigate the growth kinetics, structure, function and dynamics of multiple intermediate species populating the aggregation pathway of HEWL at pH 12.2. The different intermediates were isolated by varying the HEWL monomer concentration in the 300 nM-0.12 mM range. The intermediates were characterized using techniques like steady-state and nanosecond time-resolved fluorescence, atomic force microscopy and dynamic light scattering. Growth kinetics of non-fibrillar HEWL aggregates were fitted to the von Bertalanffy equation to yield a HEWL concentration independent rate constant (k = (6.660.6)610 25 s 21 ). Our results reveal stepwise changes in size, molecular packing and enzymatic activity among growing HEWL aggregates consistent with an isodesmic aggregation model. Formation of disulphide bonds that crosslink the monomers in the aggregate appear as a unique feature of this aggregation. AFM images of multiple amyloid fibrils emanating radially from amorphous aggregates directly confirmed that on-pathway fibril formation was feasible under isodesmic polymerization. The isolated HEWL aggregates are revealed as polycationic protein nanoparticles that are robust at neutral pH with ability to take up non-polar molecules like ANS.","downloadable_attachments":[{"id":48561100,"asset_id":7211286,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":12516997,"first_name":"Aditya","last_name":"Iyer","domain_name":"independent","page_name":"AdityaIyer2","display_name":"Aditya Iyer","profile_url":"https://independent.academia.edu/AdityaIyer2?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_22136720 coauthored" data-work_id="22136720" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/22136720/Insights_on_Channel_Like_Activity_of_Membrane_Bound_Alpha_Synuclein">Insights on Channel-Like Activity of Membrane Bound Alpha-Synuclein</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">We show via single-molecule mechanical unfolding experiments that the osmolyte glycerol stabilizes the native state of the human cardiac I27 titin module against unfolding without shifting its unfolding transition state on the mechanical... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_22136720" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">We show via single-molecule mechanical unfolding experiments that the osmolyte glycerol stabilizes the native state of the human cardiac I27 titin module against unfolding without shifting its unfolding transition state on the mechanical reaction coordinate. Taken together with similar findings on the immunoglobulin-binding domain of streptococcal protein G (GB1), these experimental results suggest that osmolytes act on proteins through a common mechanism that does not entail a shift of their unfolding transition state. We investigate the above common mechanism via an Ising-like model for protein mechanical unfolding that adds worm-like-chain behavior to a recent generalization of the Wako-Saitô -Muñ oz-Eaton model with support for group-transfer free energies. The thermodynamics of the model are exactly solvable, while protein kinetics under mechanical tension can be simulated via Monte Carlo algorithms. Notably, our force-clamp and velocity-clamp simulations exhibit no shift in the position of the unfolding transition state of GB1 and I27 under the effect of various osmolytes. The excellent agreement between experiment and simulation strongly suggests that osmolytes do not assume a structural role at the mechanical unfolding transition state of proteins, acting instead by adjusting the solvent quality for the protein chain analyte.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/22136720" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="64910e97e73f7134bf936a5958d433fa" rel="nofollow" data-download="{"attachment_id":42802319,"asset_id":22136720,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42802319/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="43466656" href="https://ucl.academia.edu/NicolettaPlotegher">Nicoletta Plotegher</a><script data-card-contents-for-user="43466656" type="text/json">{"id":43466656,"first_name":"Nicoletta","last_name":"Plotegher","domain_name":"ucl","page_name":"NicolettaPlotegher","display_name":"Nicoletta Plotegher","profile_url":"https://ucl.academia.edu/NicolettaPlotegher?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-22136720">+1</span><div class="hidden js-additional-users-22136720"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://unipd.academia.edu/LuigiBubacco">Luigi Bubacco</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-22136720'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-22136720').html(); 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container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_22136720 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="22136720"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 22136720; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=22136720]").text(description); $(".js-view-count-work_22136720").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_22136720").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="22136720"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">4</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="118582" rel="nofollow" href="https://www.academia.edu/Documents/in/Physical_sciences">Physical sciences</a>, <script data-card-contents-for-ri="118582" type="text/json">{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="260118" rel="nofollow" href="https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES">CHEMICAL SCIENCES</a><script data-card-contents-for-ri="260118" type="text/json">{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=22136720]'), work: {"id":22136720,"title":"Insights on Channel-Like Activity of Membrane Bound Alpha-Synuclein","created_at":"2016-02-18T06:07:08.228-08:00","url":"https://www.academia.edu/22136720/Insights_on_Channel_Like_Activity_of_Membrane_Bound_Alpha_Synuclein?f_ri=19156","dom_id":"work_22136720","summary":"We show via single-molecule mechanical unfolding experiments that the osmolyte glycerol stabilizes the native state of the human cardiac I27 titin module against unfolding without shifting its unfolding transition state on the mechanical reaction coordinate. Taken together with similar findings on the immunoglobulin-binding domain of streptococcal protein G (GB1), these experimental results suggest that osmolytes act on proteins through a common mechanism that does not entail a shift of their unfolding transition state. We investigate the above common mechanism via an Ising-like model for protein mechanical unfolding that adds worm-like-chain behavior to a recent generalization of the Wako-Saitô -Muñ oz-Eaton model with support for group-transfer free energies. The thermodynamics of the model are exactly solvable, while protein kinetics under mechanical tension can be simulated via Monte Carlo algorithms. Notably, our force-clamp and velocity-clamp simulations exhibit no shift in the position of the unfolding transition state of GB1 and I27 under the effect of various osmolytes. The excellent agreement between experiment and simulation strongly suggests that osmolytes do not assume a structural role at the mechanical unfolding transition state of proteins, acting instead by adjusting the solvent quality for the protein chain analyte.","downloadable_attachments":[{"id":42802319,"asset_id":22136720,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":43466656,"first_name":"Nicoletta","last_name":"Plotegher","domain_name":"ucl","page_name":"NicolettaPlotegher","display_name":"Nicoletta Plotegher","profile_url":"https://ucl.academia.edu/NicolettaPlotegher?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":33204172,"first_name":"Luigi","last_name":"Bubacco","domain_name":"unipd","page_name":"LuigiBubacco","display_name":"Luigi Bubacco","profile_url":"https://unipd.academia.edu/LuigiBubacco?f_ri=19156","photo":"https://0.academia-photos.com/33204172/11179338/12475054/s65_luigi.bubacco.jpg"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_6476895" data-work_id="6476895" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/6476895/Photobleaching_of_photosynthetic_pigments_in_spinach_thylakoid_membranes_Effect_of_temperature_oxygen_and_DCMU">Photobleaching of photosynthetic pigments in spinach thylakoid membranes. Effect of temperature, oxygen and DCMU</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The time dependence of photobleaching of photosynthetic pigments under high light illumination of isolated spinach thylakoid membranes at 22 and 4 8C was investigated. At 22 8C, the bleaching at 678, 472 and 436 nm was prominent but... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_6476895" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The time dependence of photobleaching of photosynthetic pigments under high light illumination of isolated spinach thylakoid membranes at 22 and 4 8C was investigated. At 22 8C, the bleaching at 678, 472 and 436 nm was prominent but lowering the temperature up to 4 8C during illumination prevented the pigments from bleaching almost completely. The accelerating effect on pigment photobleaching by the presence of 3-(3,4 dichlorophenyl)-1,1dimethyl-urea)-(DCMU), a well-known inhibitor of the electron transport and known to prevent photosystem I (PSI) and photosystem II (PSII) against photoinhibitory damage, was also suppressed at low temperature. At 22 8C in the presence and absence of DCMU, the decrease of the absorption at 678 and 472 nm was accompanied by a shift to the shorter wavelengths. To check the involvement of reactive oxygen species in the process, pigment photobleaching was followed in anaerobiosis. The effects of the three different environmental factors-light, temperature and DCMU-on the dynamics of photobleaching are discussed in terms of different susceptibility of the main pigment-protein complexes to photoinhibition. ᮊ</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/6476895" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="9a3d142132e07bf82f0d28e8ca4b7d2e" rel="nofollow" data-download="{"attachment_id":38315291,"asset_id":6476895,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/38315291/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="76938" href="https://bas.academia.edu/MayaVelitchkova">Maya Velitchkova</a><script data-card-contents-for-user="76938" type="text/json">{"id":76938,"first_name":"Maya","last_name":"Velitchkova","domain_name":"bas","page_name":"MayaVelitchkova","display_name":"Maya Velitchkova","profile_url":"https://bas.academia.edu/MayaVelitchkova?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_6476895 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="6476895"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 6476895, container: ".js-paper-rank-work_6476895", }); });</script></li><li class="js-percentile-work_6476895 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 6476895; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_6476895"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_6476895 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="6476895"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 6476895; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=6476895]").text(description); $(".js-view-count-work_6476895").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_6476895").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="6476895"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">20</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="5345" rel="nofollow" href="https://www.academia.edu/Documents/in/Photosynthesis">Photosynthesis</a>, <script data-card-contents-for-ri="5345" type="text/json">{"id":5345,"name":"Photosynthesis","url":"https://www.academia.edu/Documents/in/Photosynthesis?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="5427" rel="nofollow" href="https://www.academia.edu/Documents/in/Spectroscopy">Spectroscopy</a>, <script data-card-contents-for-ri="5427" type="text/json">{"id":5427,"name":"Spectroscopy","url":"https://www.academia.edu/Documents/in/Spectroscopy?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="19156" rel="nofollow" href="https://www.academia.edu/Documents/in/Biophysical_Chemistry">Biophysical Chemistry</a>, <script data-card-contents-for-ri="19156" type="text/json">{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a><script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=6476895]'), work: {"id":6476895,"title":"Photobleaching of photosynthetic pigments in spinach thylakoid membranes. Effect of temperature, oxygen and DCMU","created_at":"2014-03-19T17:16:02.366-07:00","url":"https://www.academia.edu/6476895/Photobleaching_of_photosynthetic_pigments_in_spinach_thylakoid_membranes_Effect_of_temperature_oxygen_and_DCMU?f_ri=19156","dom_id":"work_6476895","summary":"The time dependence of photobleaching of photosynthetic pigments under high light illumination of isolated spinach thylakoid membranes at 22 and 4 8C was investigated. At 22 8C, the bleaching at 678, 472 and 436 nm was prominent but lowering the temperature up to 4 8C during illumination prevented the pigments from bleaching almost completely. The accelerating effect on pigment photobleaching by the presence of 3-(3,4 dichlorophenyl)-1,1dimethyl-urea)-(DCMU), a well-known inhibitor of the electron transport and known to prevent photosystem I (PSI) and photosystem II (PSII) against photoinhibitory damage, was also suppressed at low temperature. At 22 8C in the presence and absence of DCMU, the decrease of the absorption at 678 and 472 nm was accompanied by a shift to the shorter wavelengths. To check the involvement of reactive oxygen species in the process, pigment photobleaching was followed in anaerobiosis. The effects of the three different environmental factors-light, temperature and DCMU-on the dynamics of photobleaching are discussed in terms of different susceptibility of the main pigment-protein complexes to photoinhibition. ᮊ","downloadable_attachments":[{"id":38315291,"asset_id":6476895,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":76938,"first_name":"Maya","last_name":"Velitchkova","domain_name":"bas","page_name":"MayaVelitchkova","display_name":"Maya Velitchkova","profile_url":"https://bas.academia.edu/MayaVelitchkova?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":5345,"name":"Photosynthesis","url":"https://www.academia.edu/Documents/in/Photosynthesis?f_ri=19156","nofollow":true},{"id":5427,"name":"Spectroscopy","url":"https://www.academia.edu/Documents/in/Spectroscopy?f_ri=19156","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":85564,"name":"Chlorophyll","url":"https://www.academia.edu/Documents/in/Chlorophyll?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":133177,"name":"Temperature","url":"https://www.academia.edu/Documents/in/Temperature?f_ri=19156"},{"id":144062,"name":"Pigments","url":"https://www.academia.edu/Documents/in/Pigments?f_ri=19156"},{"id":152460,"name":"Photobleaching","url":"https://www.academia.edu/Documents/in/Photobleaching?f_ri=19156"},{"id":178351,"name":"Spectrophotometry","url":"https://www.academia.edu/Documents/in/Spectrophotometry?f_ri=19156"},{"id":186094,"name":"Electron Transport","url":"https://www.academia.edu/Documents/in/Electron_Transport?f_ri=19156"},{"id":213327,"name":"photosystem I","url":"https://www.academia.edu/Documents/in/photosystem_I?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":300832,"name":"Protein Complex Detection","url":"https://www.academia.edu/Documents/in/Protein_Complex_Detection?f_ri=19156"},{"id":340112,"name":"Photosynthetic Pigment","url":"https://www.academia.edu/Documents/in/Photosynthetic_Pigment?f_ri=19156"},{"id":380825,"name":"Oxygen","url":"https://www.academia.edu/Documents/in/Oxygen?f_ri=19156"},{"id":392309,"name":"Diuron","url":"https://www.academia.edu/Documents/in/Diuron?f_ri=19156"},{"id":394477,"name":"Time Dependent","url":"https://www.academia.edu/Documents/in/Time_Dependent?f_ri=19156"},{"id":616972,"name":"Low Temperature","url":"https://www.academia.edu/Documents/in/Low_Temperature?f_ri=19156"},{"id":849801,"name":"Photosystem II","url":"https://www.academia.edu/Documents/in/Photosystem_II?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_10257756" data-work_id="10257756" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/10257756/Modeling_Zymogen_Protein_C">Modeling Zymogen Protein C</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">A solution structure for the complete zymogen form of human coagulation protein C is modeled. The initial core structure is based on the x-ray crystallographic structure of the ␥-carboxyglutamic acid (Gla)-domainless activated form. The... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_10257756" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">A solution structure for the complete zymogen form of human coagulation protein C is modeled. The initial core structure is based on the x-ray crystallographic structure of the ␥-carboxyglutamic acid (Gla)-domainless activated form. The Gla domain (residues 1-48) is modeled from the x-ray crystal coordinates of the factor VII a /tissue factor complex and oriented with the epidermal growth factor-1 domain to yield an initial orientation consistent with the x-ray crystal structure of porcine factor IX a . The missing C-terminal residues in the light chain (residues 147-157) and the activation peptide residues 158 -169 were introduced using homology modeling so that the activation peptide residues directly interact with the residues in the calcium binding loop. Molecular dynamics simulations (Amber-particle-mesh-Ewald) are used to obtain the complete calcium-complexed solution structure. The individual domain structures of protein C in solution are largely unaffected by solvation, whereas the Gla-epidermal growth factor-1 orientation evolves to a form different from both factors VII a and IX a . The solution structure of the zymogen protein C is compared with the crystal structures of the existing zymogen serine proteases: chymotrypsinogen, proproteinase, and prethrombin-2. Calculated electrostatic potential surfaces support the involvement of the serine protease calcium ion binding loop in providing a suitable electrostatic environment around the scissile bond for II a /thrombomodulin interaction.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/10257756" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="e3a81f518702c04deff9226dc58ef957" rel="nofollow" data-download="{"attachment_id":36344656,"asset_id":10257756,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/36344656/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="25115310" href="https://independent.academia.edu/PereraLalith">Lalith Perera</a><script data-card-contents-for-user="25115310" type="text/json">{"id":25115310,"first_name":"Lalith","last_name":"Perera","domain_name":"independent","page_name":"PereraLalith","display_name":"Lalith Perera","profile_url":"https://independent.academia.edu/PereraLalith?f_ri=19156","photo":"https://0.academia-photos.com/25115310/6827343/7706345/s65_lalith.perera.jpg"}</script></span></span></li><li class="js-paper-rank-work_10257756 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="10257756"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 10257756, container: ".js-paper-rank-work_10257756", }); 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The initial core structure is based on the x-ray crystallographic structure of the ␥-carboxyglutamic acid (Gla)-domainless activated form. The Gla domain (residues 1-48) is modeled from the x-ray crystal coordinates of the factor VII a /tissue factor complex and oriented with the epidermal growth factor-1 domain to yield an initial orientation consistent with the x-ray crystal structure of porcine factor IX a . The missing C-terminal residues in the light chain (residues 147-157) and the activation peptide residues 158 -169 were introduced using homology modeling so that the activation peptide residues directly interact with the residues in the calcium binding loop. Molecular dynamics simulations (Amber-particle-mesh-Ewald) are used to obtain the complete calcium-complexed solution structure. The individual domain structures of protein C in solution are largely unaffected by solvation, whereas the Gla-epidermal growth factor-1 orientation evolves to a form different from both factors VII a and IX a . The solution structure of the zymogen protein C is compared with the crystal structures of the existing zymogen serine proteases: chymotrypsinogen, proproteinase, and prethrombin-2. Calculated electrostatic potential surfaces support the involvement of the serine protease calcium ion binding loop in providing a suitable electrostatic environment around the scissile bond for II a /thrombomodulin interaction.","downloadable_attachments":[{"id":36344656,"asset_id":10257756,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":25115310,"first_name":"Lalith","last_name":"Perera","domain_name":"independent","page_name":"PereraLalith","display_name":"Lalith Perera","profile_url":"https://independent.academia.edu/PereraLalith?f_ri=19156","photo":"https://0.academia-photos.com/25115310/6827343/7706345/s65_lalith.perera.jpg"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography?f_ri=19156","nofollow":true},{"id":46256,"name":"Homology Modeling","url":"https://www.academia.edu/Documents/in/Homology_Modeling?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":50630,"name":"Crystal structure","url":"https://www.academia.edu/Documents/in/Crystal_structure?f_ri=19156"},{"id":56001,"name":"X Rays","url":"https://www.academia.edu/Documents/in/X_Rays?f_ri=19156"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156"},{"id":329263,"name":"Epidermal Growth Factor","url":"https://www.academia.edu/Documents/in/Epidermal_Growth_Factor?f_ri=19156"},{"id":414692,"name":"Solutions","url":"https://www.academia.edu/Documents/in/Solutions?f_ri=19156"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation?f_ri=19156"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence?f_ri=19156"},{"id":1154758,"name":"Serine Protease","url":"https://www.academia.edu/Documents/in/Serine_Protease?f_ri=19156"},{"id":1156199,"name":"Tissue Factor","url":"https://www.academia.edu/Documents/in/Tissue_Factor?f_ri=19156"},{"id":1242504,"name":"Molecular Dynamic Simulation","url":"https://www.academia.edu/Documents/in/Molecular_Dynamic_Simulation?f_ri=19156"},{"id":1312081,"name":"Light chain","url":"https://www.academia.edu/Documents/in/Light_chain?f_ri=19156"},{"id":1333505,"name":"Solution Structure","url":"https://www.academia.edu/Documents/in/Solution_Structure?f_ri=19156"},{"id":1912157,"name":"Domain Structure","url":"https://www.academia.edu/Documents/in/Domain_Structure?f_ri=19156"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_13639165" data-work_id="13639165" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/13639165/Characterization_of_human_embryonic_stem_cell_lines_by_the_International_Stem_Cell_Initiative">Characterization of human embryonic stem cell lines by the International Stem Cell Initiative</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The International Stem Cell Initiative characterized 59 human embryonic stem cell lines from 17 laboratories worldwide. Despite diverse genotypes and different techniques used for derivation and maintenance, all lines exhibited similar... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_13639165" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The International Stem Cell Initiative characterized 59 human embryonic stem cell lines from 17 laboratories worldwide. Despite diverse genotypes and different techniques used for derivation and maintenance, all lines exhibited similar expression patterns for several markers of human embryonic stem cells. They expressed the glycolipid antigens SSEA3 and SSEA4, the keratan sulfate antigens TRA-1-60, TRA-1-81, GCTM2 and GCT343, and the protein antigens CD9, Thy1 (also known as CD90), tissue-nonspecific alkaline phosphatase and class 1 HLA, as well as the strongly developmentally regulated genes NANOG, POU5F1 (formerly known as OCT4), TDGF1, DNMT3B, GABRB3 and GDF3. Nevertheless, the lines were not identical: differences in expression of several lineage markers were evident, and several imprinted genes showed generally similar allelespecific expression patterns, but some gene-dependent variation was observed. Also, some female lines expressed readily detectable levels of XIST whereas others did not. No significant contamination of the lines with mycoplasma, bacteria or cytopathic viruses was detected.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/13639165" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="c55b327ac13357aefcb601c1f5ad707d" rel="nofollow" data-download="{"attachment_id":45119562,"asset_id":13639165,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/45119562/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32798326" href="https://helsinki.academia.edu/TimoOtonkoski">Timo Otonkoski</a><script data-card-contents-for-user="32798326" type="text/json">{"id":32798326,"first_name":"Timo","last_name":"Otonkoski","domain_name":"helsinki","page_name":"TimoOtonkoski","display_name":"Timo Otonkoski","profile_url":"https://helsinki.academia.edu/TimoOtonkoski?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_13639165 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="13639165"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 13639165, container: ".js-paper-rank-work_13639165", }); 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Despite diverse genotypes and different techniques used for derivation and maintenance, all lines exhibited similar expression patterns for several markers of human embryonic stem cells. They expressed the glycolipid antigens SSEA3 and SSEA4, the keratan sulfate antigens TRA-1-60, TRA-1-81, GCTM2 and GCT343, and the protein antigens CD9, Thy1 (also known as CD90), tissue-nonspecific alkaline phosphatase and class 1 HLA, as well as the strongly developmentally regulated genes NANOG, POU5F1 (formerly known as OCT4), TDGF1, DNMT3B, GABRB3 and GDF3. Nevertheless, the lines were not identical: differences in expression of several lineage markers were evident, and several imprinted genes showed generally similar allelespecific expression patterns, but some gene-dependent variation was observed. Also, some female lines expressed readily detectable levels of XIST whereas others did not. No significant contamination of the lines with mycoplasma, bacteria or cytopathic viruses was detected.","downloadable_attachments":[{"id":45119562,"asset_id":13639165,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32798326,"first_name":"Timo","last_name":"Otonkoski","domain_name":"helsinki","page_name":"TimoOtonkoski","display_name":"Timo Otonkoski","profile_url":"https://helsinki.academia.edu/TimoOtonkoski?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics?f_ri=19156","nofollow":true},{"id":173,"name":"Zoology","url":"https://www.academia.edu/Documents/in/Zoology?f_ri=19156","nofollow":true},{"id":3642,"name":"Stem Cells","url":"https://www.academia.edu/Documents/in/Stem_Cells?f_ri=19156","nofollow":true},{"id":3643,"name":"Human Embryonic Stem 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class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_13769349 coauthored" data-work_id="13769349" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/13769349/Inactivation_of_the_Bacterial_Mechanosensitive_Channel_MscL_Involves_Flexible_Transmembrane_Helices_and_a_Dry_Gate">Inactivation of the Bacterial Mechanosensitive Channel MscL Involves Flexible Transmembrane Helices and a ‘Dry’Gate</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">whether Cav1.2 channels are mechanosensitive and the possible role of integrins in this process, patch clamp methods were used to investigate the properties of either native or heterologously expressed Cav1.2 cannels by stretch of single... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_13769349" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">whether Cav1.2 channels are mechanosensitive and the possible role of integrins in this process, patch clamp methods were used to investigate the properties of either native or heterologously expressed Cav1.2 cannels by stretch of single cells plated onto a flexible substrate. Thin silicone membranes were coated with either fibronectin (FN) or poly-l-lysine (PLL) to assess integrin-dependent and -independent responses, respectively, and stretched using two blunt micropipettes driven in equal and opposite directions by piezoelectric translators. Graded stretch to 130% of resting cell length induced graded increases in Cav1.2 current (up to 63%) in HEK 293 cells expressing the neuronal channel isoform (Cav1.2c). The increase in current was~2-fold greater for cells adhering to FN than for cells on PLL. On FN, 130% longitudinal stretch of primary VSM cells induced~50% increases in Cav1.2 current. However, the magnitude of stretch-activated Cav1.2 current was the same on FN or PLL for cells expressing a Cav1.2 construct containing two C-terminal mutations (Y2122F/S1901A) to prevent phosphorylation by PKA and c-Src, or for cells expressing a Cav1.2 construct with the C-terminus truncated. Our results suggest that the Cav1.2 channel can be potentiated by membrane stretch, with one component due to intrinsic mechanosensitivity of the channel and a second component due to signaling through an integrin-dependent process.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/13769349" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="f9ed38311065282d400ea5a809e60348" rel="nofollow" data-download="{"attachment_id":44974167,"asset_id":13769349,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/44974167/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32880372" href="https://umcp.academia.edu/AndriyAnishkin">Andriy Anishkin</a><script data-card-contents-for-user="32880372" type="text/json">{"id":32880372,"first_name":"Andriy","last_name":"Anishkin","domain_name":"umcp","page_name":"AndriyAnishkin","display_name":"Andriy Anishkin","profile_url":"https://umcp.academia.edu/AndriyAnishkin?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-13769349">+1</span><div class="hidden js-additional-users-13769349"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://umd.academia.edu/SergeiSukharev">Sergei Sukharev</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-13769349'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-13769349').html(); 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Thin silicone membranes were coated with either fibronectin (FN) or poly-l-lysine (PLL) to assess integrin-dependent and -independent responses, respectively, and stretched using two blunt micropipettes driven in equal and opposite directions by piezoelectric translators. Graded stretch to 130% of resting cell length induced graded increases in Cav1.2 current (up to 63%) in HEK 293 cells expressing the neuronal channel isoform (Cav1.2c). The increase in current was~2-fold greater for cells adhering to FN than for cells on PLL. On FN, 130% longitudinal stretch of primary VSM cells induced~50% increases in Cav1.2 current. However, the magnitude of stretch-activated Cav1.2 current was the same on FN or PLL for cells expressing a Cav1.2 construct containing two C-terminal mutations (Y2122F/S1901A) to prevent phosphorylation by PKA and c-Src, or for cells expressing a Cav1.2 construct with the C-terminus truncated. Our results suggest that the Cav1.2 channel can be potentiated by membrane stretch, with one component due to intrinsic mechanosensitivity of the channel and a second component due to signaling through an integrin-dependent process.","downloadable_attachments":[{"id":44974167,"asset_id":13769349,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32880372,"first_name":"Andriy","last_name":"Anishkin","domain_name":"umcp","page_name":"AndriyAnishkin","display_name":"Andriy Anishkin","profile_url":"https://umcp.academia.edu/AndriyAnishkin?f_ri=19156","photo":"/images/s65_no_pic.png"},{"id":32819717,"first_name":"Sergei","last_name":"Sukharev","domain_name":"umd","page_name":"SergeiSukharev","display_name":"Sergei Sukharev","profile_url":"https://umd.academia.edu/SergeiSukharev?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=19156","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=19156","nofollow":true},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=19156","nofollow":true}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_15442806" data-work_id="15442806" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/15442806/Laparoscopic_Management_of_Juvenile_Cystic_Adenomyoma_A_Rare_Cause_of_Dysmenorrhea">Laparoscopic Management of Juvenile Cystic Adenomyoma – A Rare Cause of Dysmenorrhea</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Two cases of juvenile cystic adenomyoma of the uterus treated by laparoscopic surgery are reported. Preoperative diagnostic imaging procedures located a cystic structure within the uterine nodule of each of these young women with severe... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_15442806" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Two cases of juvenile cystic adenomyoma of the uterus treated by laparoscopic surgery are reported. Preoperative diagnostic imaging procedures located a cystic structure within the uterine nodule of each of these young women with severe dysmenorrhea. Under a diagnosis of cystic adenomyoma, laparoscopic excision was performed. Histopathologic examination of the resected tissues showed the presence of an endometrial structure composed of epithelium and stroma within myometrial nodule. In both of these patients, dysmenorrhea disappeared postoperatively.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/15442806" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="2d7fb26175916522226f263f5d07e89e" rel="nofollow" data-download="{"attachment_id":43193197,"asset_id":15442806,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/43193197/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="34428359" href="https://independent.academia.edu/NeerjaBhatla">Neerja Bhatla</a><script data-card-contents-for-user="34428359" type="text/json">{"id":34428359,"first_name":"Neerja","last_name":"Bhatla","domain_name":"independent","page_name":"NeerjaBhatla","display_name":"Neerja Bhatla","profile_url":"https://independent.academia.edu/NeerjaBhatla?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_15442806 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="15442806"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 15442806, container: ".js-paper-rank-work_15442806", }); 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Preoperative diagnostic imaging procedures located a cystic structure within the uterine nodule of each of these young women with severe dysmenorrhea. Under a diagnosis of cystic adenomyoma, laparoscopic excision was performed. Histopathologic examination of the resected tissues showed the presence of an endometrial structure composed of epithelium and stroma within myometrial nodule. In both of these patients, dysmenorrhea disappeared postoperatively.","downloadable_attachments":[{"id":43193197,"asset_id":15442806,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":34428359,"first_name":"Neerja","last_name":"Bhatla","domain_name":"independent","page_name":"NeerjaBhatla","display_name":"Neerja Bhatla","profile_url":"https://independent.academia.edu/NeerjaBhatla?f_ri=19156","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=19156","nofollow":true},{"id":22506,"name":"Adolescent","url":"https://www.academia.edu/Documents/in/Adolescent?f_ri=19156","nofollow":true},{"id":133057,"name":"Young Adult","url":"https://www.academia.edu/Documents/in/Young_Adult?f_ri=19156","nofollow":true},{"id":471037,"name":"Dysmenorrhea","url":"https://www.academia.edu/Documents/in/Dysmenorrhea?f_ri=19156","nofollow":true},{"id":1229542,"name":"Laparoscopy","url":"https://www.academia.edu/Documents/in/Laparoscopy?f_ri=19156"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_16254084 coauthored" data-work_id="16254084" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/16254084/Biophysical_science_in_Italy_SIBPA_turns_40">Biophysical science in Italy: SIBPA turns 40</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Topics cover all biophysical disciplines, from molecular to cellular, to integrative biophysics giving an almost comprehensive view of the interdisciplinary and multidisciplinary approaches, proper of the modern biophysics. SIBPA, which... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_16254084" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Topics cover all biophysical disciplines, from molecular to cellular, to integrative biophysics giving an almost comprehensive view of the interdisciplinary and multidisciplinary approaches, proper of the modern biophysics. 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In particular, we model the crenated, echinocytic shapes and show how they may arise from a competition between the bending energy of the plasma membrane and the... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_71518459" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">We study the shapes of human red blood cells using continuum mechanics. In particular, we model the crenated, echinocytic shapes and show how they may arise from a competition between the bending energy of the plasma membrane and the stretching/shear elastic energies of ...</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/71518459" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="4b45e9c6a4454a743db4127d0a0123eb" rel="nofollow" data-download="{"attachment_id":80826478,"asset_id":71518459,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/80826478/download_file?st=MTczOTg1NTM5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="112900206" href="https://clarku.academia.edu/RanjanMukhopadhyay">Ranjan Mukhopadhyay</a><script data-card-contents-for-user="112900206" type="text/json">{"id":112900206,"first_name":"Ranjan","last_name":"Mukhopadhyay","domain_name":"clarku","page_name":"RanjanMukhopadhyay","display_name":"Ranjan Mukhopadhyay","profile_url":"https://clarku.academia.edu/RanjanMukhopadhyay?f_ri=19156","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_71518459 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="71518459"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 71518459, container: ".js-paper-rank-work_71518459", }); 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