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Protein tertiary structure - Wikipedia
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<span>Determinants</span> </div> </a> <button aria-controls="toc-Determinants-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Determinants subsection</span> </button> <ul id="toc-Determinants-sublist" class="vector-toc-list"> <li id="toc-Stability_of_native_states" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Stability_of_native_states"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Stability of native states</span> </div> </a> <ul id="toc-Stability_of_native_states-sublist" class="vector-toc-list"> <li id="toc-Thermostability" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Thermostability"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1.1</span> <span>Thermostability</span> </div> </a> <ul id="toc-Thermostability-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Kinetic_traps" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Kinetic_traps"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1.2</span> <span>Kinetic traps</span> </div> </a> <ul id="toc-Kinetic_traps-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Metastability" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Metastability"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1.3</span> <span>Metastability</span> </div> </a> <ul id="toc-Metastability-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Chaperone_proteins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chaperone_proteins"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Chaperone proteins</span> </div> </a> <ul id="toc-Chaperone_proteins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cytoplasmic_environment" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cytoplasmic_environment"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Cytoplasmic environment</span> </div> </a> <ul id="toc-Cytoplasmic_environment-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Ligand_binding" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Ligand_binding"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Ligand binding</span> </div> </a> <ul id="toc-Ligand_binding-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Determination" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Determination"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Determination</span> </div> </a> <button aria-controls="toc-Determination-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Determination subsection</span> </button> <ul id="toc-Determination-sublist" class="vector-toc-list"> <li id="toc-X-ray_crystallography" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#X-ray_crystallography"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.1</span> <span>X-ray crystallography</span> </div> </a> <ul id="toc-X-ray_crystallography-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-NMR" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#NMR"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.2</span> <span>NMR</span> </div> </a> <ul id="toc-NMR-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cryogenic_electron_microscopy" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cryogenic_electron_microscopy"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.3</span> <span>Cryogenic electron microscopy</span> </div> </a> <ul id="toc-Cryogenic_electron_microscopy-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Dual_polarisation_interferometry" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Dual_polarisation_interferometry"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.4</span> <span>Dual polarisation interferometry</span> </div> </a> <ul id="toc-Dual_polarisation_interferometry-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Projects" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Projects"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Projects</span> </div> </a> <button aria-controls="toc-Projects-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Projects subsection</span> </button> <ul id="toc-Projects-sublist" class="vector-toc-list"> <li id="toc-Prediction_algorithm" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Prediction_algorithm"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Prediction algorithm</span> </div> </a> <ul id="toc-Prediction_algorithm-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Protein_aggregation_diseases" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Protein_aggregation_diseases"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Protein aggregation diseases</span> </div> </a> <ul id="toc-Protein_aggregation_diseases-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Protein_Tertiary_Structure_Retrieval_Project_(CoMOGrad)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Protein_Tertiary_Structure_Retrieval_Project_(CoMOGrad)"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.3</span> <span>Protein Tertiary Structure Retrieval Project (CoMOGrad)</span> </div> </a> <ul id="toc-Protein_Tertiary_Structure_Retrieval_Project_(CoMOGrad)-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-listBullet mw-ui-icon-wikimedia-listBullet"></span> <span class="vector-dropdown-label-text">Toggle the table of contents</span> </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Protein tertiary structure</span></h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 27 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-27" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">27 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D8%A8%D9%86%D9%8A%D8%A9_%D8%A8%D8%B1%D9%88%D8%AA%D9%8A%D9%86_%D8%AB%D8%A7%D9%84%D8%AB%D9%8A%D8%A9" title="بنية بروتين ثالثية – Arabic" lang="ar" hreflang="ar" data-title="بنية بروتين ثالثية" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Tercijarna_struktura_proteina" title="Tercijarna struktura proteina – Bosnian" lang="bs" hreflang="bs" data-title="Tercijarna struktura proteina" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Estructura_terci%C3%A0ria_de_les_prote%C3%AFnes" title="Estructura terciària de les proteïnes – Catalan" lang="ca" hreflang="ca" data-title="Estructura terciària de les proteïnes" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Terti%C3%A4rstruktur" title="Tertiärstruktur – German" lang="de" hreflang="de" data-title="Tertiärstruktur" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-el mw-list-item"><a href="https://el.wikipedia.org/wiki/%CE%A4%CF%81%CE%B9%CF%84%CE%BF%CF%84%CE%B1%CE%B3%CE%AE%CF%82_%CE%B4%CE%BF%CE%BC%CE%AE_%CF%80%CF%81%CF%89%CF%84%CE%B5%CE%90%CE%BD%CE%B7%CF%82" title="Τριτοταγής δομή πρωτεΐνης – Greek" lang="el" hreflang="el" data-title="Τριτοταγής δομή πρωτεΐνης" data-language-autonym="Ελληνικά" data-language-local-name="Greek" class="interlanguage-link-target"><span>Ελληνικά</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Estructura_terciaria_de_las_prote%C3%ADnas" title="Estructura terciaria de las proteínas – Spanish" lang="es" hreflang="es" data-title="Estructura terciaria de las proteínas" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-eo mw-list-item"><a href="https://eo.wikipedia.org/wiki/Terciara_strukturo" title="Terciara strukturo – Esperanto" lang="eo" hreflang="eo" data-title="Terciara strukturo" data-language-autonym="Esperanto" data-language-local-name="Esperanto" class="interlanguage-link-target"><span>Esperanto</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Structure_tertiaire" title="Structure tertiaire – French" lang="fr" hreflang="fr" data-title="Structure tertiaire" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Estrutura_terciaria_das_prote%C3%ADnas" title="Estrutura terciaria das proteínas – Galician" lang="gl" hreflang="gl" data-title="Estrutura terciaria das proteínas" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EB%8B%A8%EB%B0%B1%EC%A7%88%EC%9D%98_3%EC%B0%A8_%EA%B5%AC%EC%A1%B0" title="단백질의 3차 구조 – Korean" lang="ko" hreflang="ko" data-title="단백질의 3차 구조" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Struttura_terziaria" title="Struttura terziaria – Italian" lang="it" hreflang="it" data-title="Struttura terziaria" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-he mw-list-item"><a href="https://he.wikipedia.org/wiki/%D7%9E%D7%91%D7%A0%D7%94_%D7%A9%D7%9C%D7%99%D7%A9%D7%95%D7%A0%D7%99" title="מבנה שלישוני – Hebrew" lang="he" hreflang="he" data-title="מבנה שלישוני" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-mk mw-list-item"><a href="https://mk.wikipedia.org/wiki/%D0%A2%D1%80%D0%B5%D1%82%D0%B8%D1%87%D0%BD%D0%B0_%D1%81%D1%82%D1%80%D1%83%D0%BA%D1%82%D1%83%D1%80%D0%B0_%D0%BD%D0%B0_%D0%B1%D0%B5%D0%BB%D0%BA%D0%BE%D0%B2%D0%B8%D0%BD%D0%B8%D1%82%D0%B5" title="Третична структура на белковините – Macedonian" lang="mk" hreflang="mk" data-title="Третична структура на белковините" data-language-autonym="Македонски" data-language-local-name="Macedonian" class="interlanguage-link-target"><span>Македонски</span></a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Struktur_tertier_protein" title="Struktur tertier protein – Malay" lang="ms" hreflang="ms" data-title="Struktur tertier protein" data-language-autonym="Bahasa Melayu" data-language-local-name="Malay" class="interlanguage-link-target"><span>Bahasa Melayu</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Tertiaire_structuur_(eiwitten)" title="Tertiaire structuur (eiwitten) – Dutch" lang="nl" hreflang="nl" data-title="Tertiaire structuur (eiwitten)" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E4%B8%89%E6%AC%A1%E6%A7%8B%E9%80%A0" title="三次構造 – Japanese" lang="ja" hreflang="ja" data-title="三次構造" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-uz mw-list-item"><a href="https://uz.wikipedia.org/wiki/Oqsilning_uchlamchi_strukturasi" title="Oqsilning uchlamchi strukturasi – Uzbek" lang="uz" hreflang="uz" data-title="Oqsilning uchlamchi strukturasi" data-language-autonym="Oʻzbekcha / ўзбекча" data-language-local-name="Uzbek" class="interlanguage-link-target"><span>Oʻzbekcha / ўзбекча</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Struktura_trzeciorz%C4%99dowa_bia%C5%82ka" title="Struktura trzeciorzędowa białka – Polish" lang="pl" hreflang="pl" data-title="Struktura trzeciorzędowa białka" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Estrutura_terci%C3%A1ria_da_prote%C3%ADna" title="Estrutura terciária da proteína – Portuguese" lang="pt" hreflang="pt" data-title="Estrutura terciária da proteína" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%A2%D1%80%D0%B5%D1%82%D0%B8%D1%87%D0%BD%D0%B0%D1%8F_%D1%81%D1%82%D1%80%D1%83%D0%BA%D1%82%D1%83%D1%80%D0%B0" title="Третичная структура – Russian" lang="ru" hreflang="ru" data-title="Третичная структура" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/%D0%A2%D0%B5%D1%80%D1%86%D0%B8%D1%98%D0%B0%D1%80%D0%BD%D0%B0_%D1%81%D1%82%D1%80%D1%83%D0%BA%D1%82%D1%83%D1%80%D0%B0_%D0%BF%D1%80%D0%BE%D1%82%D0%B5%D0%B8%D0%BD%D0%B0" title="Терцијарна структура протеина – Serbian" lang="sr" hreflang="sr" data-title="Терцијарна структура протеина" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Tercijarna_struktura_proteina" title="Tercijarna struktura proteina – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Tercijarna struktura proteina" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Terti%C3%A4rstruktur" title="Tertiärstruktur – Swedish" lang="sv" hreflang="sv" data-title="Tertiärstruktur" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%A2%D1%80%D0%B5%D1%82%D0%B8%D0%BD%D0%BD%D0%B0_%D1%81%D1%82%D1%80%D1%83%D0%BA%D1%82%D1%83%D1%80%D0%B0_%D0%B1%D1%96%D0%BB%D0%BA%D1%96%D0%B2" title="Третинна структура білків – Ukrainian" lang="uk" hreflang="uk" data-title="Третинна структура білків" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target"><span>Українська</span></a></li><li class="interlanguage-link interwiki-vi mw-list-item"><a href="https://vi.wikipedia.org/wiki/C%E1%BA%A5u_tr%C3%BAc_b%E1%BA%ADc_ba_c%E1%BB%A7a_protein" title="Cấu trúc bậc ba của protein – Vietnamese" lang="vi" hreflang="vi" data-title="Cấu trúc bậc ba của protein" data-language-autonym="Tiếng Việt" data-language-local-name="Vietnamese" class="interlanguage-link-target"><span>Tiếng Việt</span></a></li><li class="interlanguage-link interwiki-wuu mw-list-item"><a href="https://wuu.wikipedia.org/wiki/%E8%9B%8B%E7%99%BD%E8%B4%A8%E4%B8%89%E7%BA%A7%E7%BB%93%E6%9E%84" 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structure</a>)</span></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Three dimensional shape of a protein</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">This article is about tertiary structure in protein. For the article about tertiary structure in nucleic acid, see <a href="/wiki/Nucleic_acid_tertiary_structure" title="Nucleic acid tertiary structure">Nucleic acid tertiary structure</a>.</div> <style data-mw-deduplicate="TemplateStyles:r1251242444">.mw-parser-output .ambox{border:1px solid #a2a9b1;border-left:10px solid #36c;background-color:#fbfbfb;box-sizing:border-box}.mw-parser-output .ambox+link+.ambox,.mw-parser-output .ambox+link+style+.ambox,.mw-parser-output .ambox+link+link+.ambox,.mw-parser-output .ambox+.mw-empty-elt+link+.ambox,.mw-parser-output .ambox+.mw-empty-elt+link+style+.ambox,.mw-parser-output .ambox+.mw-empty-elt+link+link+.ambox{margin-top:-1px}html body.mediawiki .mw-parser-output .ambox.mbox-small-left{margin:4px 1em 4px 0;overflow:hidden;width:238px;border-collapse:collapse;font-size:88%;line-height:1.25em}.mw-parser-output .ambox-speedy{border-left:10px solid #b32424;background-color:#fee7e6}.mw-parser-output .ambox-delete{border-left:10px solid #b32424}.mw-parser-output .ambox-content{border-left:10px solid #f28500}.mw-parser-output .ambox-style{border-left:10px solid #fc3}.mw-parser-output .ambox-move{border-left:10px solid #9932cc}.mw-parser-output .ambox-protection{border-left:10px solid #a2a9b1}.mw-parser-output .ambox .mbox-text{border:none;padding:0.25em 0.5em;width:100%}.mw-parser-output .ambox .mbox-image{border:none;padding:2px 0 2px 0.5em;text-align:center}.mw-parser-output .ambox .mbox-imageright{border:none;padding:2px 0.5em 2px 0;text-align:center}.mw-parser-output .ambox .mbox-empty-cell{border:none;padding:0;width:1px}.mw-parser-output .ambox .mbox-image-div{width:52px}@media(min-width:720px){.mw-parser-output .ambox{margin:0 10%}}@media print{body.ns-0 .mw-parser-output .ambox{display:none!important}}</style><table class="box-More_citations_needed plainlinks metadata ambox ambox-content ambox-Refimprove" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><a href="/wiki/File:Question_book-new.svg" class="mw-file-description"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/9/99/Question_book-new.svg/50px-Question_book-new.svg.png" decoding="async" width="50" height="39" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/9/99/Question_book-new.svg/75px-Question_book-new.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/9/99/Question_book-new.svg/100px-Question_book-new.svg.png 2x" data-file-width="512" data-file-height="399" /></a></span></div></td><td class="mbox-text"><div class="mbox-text-span">This article <b>needs additional citations for <a href="/wiki/Wikipedia:Verifiability" title="Wikipedia:Verifiability">verification</a></b>.<span class="hide-when-compact"> Please help <a href="/wiki/Special:EditPage/Protein_tertiary_structure" title="Special:EditPage/Protein tertiary structure">improve this article</a> by <a href="/wiki/Help:Referencing_for_beginners" title="Help:Referencing for beginners">adding citations to reliable sources</a>. Unsourced material may be challenged and removed.<br /><small><span class="plainlinks"><i>Find sources:</i> <a rel="nofollow" class="external text" href="https://www.google.com/search?as_eq=wikipedia&q=%22Protein+tertiary+structure%22">"Protein tertiary structure"</a> – <a rel="nofollow" class="external text" href="https://www.google.com/search?tbm=nws&q=%22Protein+tertiary+structure%22+-wikipedia&tbs=ar:1">news</a> <b>·</b> <a rel="nofollow" class="external text" href="https://www.google.com/search?&q=%22Protein+tertiary+structure%22&tbs=bkt:s&tbm=bks">newspapers</a> <b>·</b> <a rel="nofollow" class="external text" href="https://www.google.com/search?tbs=bks:1&q=%22Protein+tertiary+structure%22+-wikipedia">books</a> <b>·</b> <a rel="nofollow" class="external text" href="https://scholar.google.com/scholar?q=%22Protein+tertiary+structure%22">scholar</a> <b>·</b> <a rel="nofollow" class="external text" href="https://www.jstor.org/action/doBasicSearch?Query=%22Protein+tertiary+structure%22&acc=on&wc=on">JSTOR</a></span></small></span> <span class="date-container"><i>(<span class="date">December 2013</span>)</i></span><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> <figure class="noresize" typeof="mw:File/Thumb"><span><img src="//upload.wikimedia.org/wikipedia/commons/thumb/5/5e/Protein_structure_%283%29-en.svg/270px-Protein_structure_%283%29-en.svg.png" decoding="async" width="270" height="439" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/5/5e/Protein_structure_%283%29-en.svg/405px-Protein_structure_%283%29-en.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/5/5e/Protein_structure_%283%29-en.svg/540px-Protein_structure_%283%29-en.svg.png 2x" data-file-width="2950" data-file-height="4800" usemap="#ImageMap_7475d4ee38a50cbd" resource="/wiki/File:Protein_structure_(3)-en.svg" /></span><map name="ImageMap_7475d4ee38a50cbd"><area href="/wiki/Protein_primary_structure" shape="rect" coords="0,0,288,64" alt="Protein primary structure" title="Protein primary structure" /><area href="/wiki/Protein_secondary_structure" shape="rect" coords="0,64,288,130" alt="Protein secondary structure" title="Protein secondary structure" /><area href="/wiki/Protein_tertiary_structure" shape="rect" coords="0,130,288,230" alt="Protein tertiary structure" title="Protein tertiary structure" /><area href="/wiki/Protein_quaternary_structure" shape="rect" coords="0,230,288,470" alt="Protein quaternary structure" title="Protein quaternary structure" /></map><figcaption><figure class="mw-halign-left" typeof="mw:File"><span title="The image above contains clickable links"><img alt="The image above contains clickable links" src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e6/Interactive_icon.svg/18px-Interactive_icon.svg.png" decoding="async" width="18" height="27" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e6/Interactive_icon.svg/27px-Interactive_icon.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e6/Interactive_icon.svg/36px-Interactive_icon.svg.png 2x" data-file-width="133" data-file-height="200" /></span><figcaption>The image above contains clickable links</figcaption></figure> <a href="https://commons.wikimedia.org/wiki/File:Protein_structure_(3)-en.svg" class="extiw" title="c:File:Protein structure (3)-en.svg">This diagram</a> (which is interactive) of <a href="/wiki/Protein_structure" title="Protein structure">protein structure</a> uses <a href="/wiki/PCNA" class="mw-redirect" title="PCNA">PCNA</a> as an example. (<span class="plainlinks"><a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1AXC">1AXC</a></span>)</figcaption></figure> <figure typeof="mw:File/Frame"><a href="/wiki/File:Tertiary_Structure_of_a_Protein.svg" class="mw-file-description"><img alt="Tertiary Structure of a Protein" src="//upload.wikimedia.org/wikipedia/commons/thumb/4/40/Tertiary_Structure_of_a_Protein.svg/512px-Tertiary_Structure_of_a_Protein.svg.png" decoding="async" width="512" height="297" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/40/Tertiary_Structure_of_a_Protein.svg/768px-Tertiary_Structure_of_a_Protein.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/40/Tertiary_Structure_of_a_Protein.svg/1024px-Tertiary_Structure_of_a_Protein.svg.png 2x" data-file-width="512" data-file-height="297" /></a><figcaption>The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions.</figcaption></figure> <p><b>Protein tertiary structure</b> is the three-dimensional shape of a <a href="/wiki/Protein" title="Protein">protein</a>. The tertiary structure will have a single <a href="/wiki/Polypeptide" class="mw-redirect" title="Polypeptide">polypeptide</a> chain "backbone" with one or more <a href="/wiki/Protein_secondary_structure" title="Protein secondary structure">protein secondary structures</a>, the <a href="/wiki/Protein_domain" title="Protein domain">protein domains</a>. <a href="/wiki/Amino_acid" title="Amino acid">Amino acid</a> <a href="/wiki/Side_chain" title="Side chain">side chains</a> and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its <a href="/wiki/Atom" title="Atom">atomic</a> coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-bran_2-0" class="reference"><a href="#cite_note-bran-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> A number of these structures may bind to each other, forming a <a href="/wiki/Protein_quaternary_structure" title="Protein quaternary structure">quaternary structure</a>.<sup id="cite_ref-kyte_3-0" class="reference"><a href="#cite_note-kyte-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="History">History</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=1" title="Edit section: History"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The science of the tertiary structure of proteins has progressed from one of <a href="/wiki/Hypothesis" title="Hypothesis">hypothesis</a> to one of detailed definition. Although <a href="/wiki/Hermann_Emil_Fischer" class="mw-redirect" title="Hermann Emil Fischer">Emil Fischer</a> had suggested proteins were made of <a href="/wiki/Polypeptide_chain" class="mw-redirect" title="Polypeptide chain">polypeptide chains</a> and amino acid side chains, it was <a href="/wiki/Dorothy_Maud_Wrinch" title="Dorothy Maud Wrinch">Dorothy Maud Wrinch</a> who incorporated <a href="/wiki/Geometry" title="Geometry">geometry</a> into the prediction of <a href="/wiki/Protein_structure" title="Protein structure">protein structures</a>. Wrinch demonstrated this with the <a href="/wiki/Cyclol" title="Cyclol"><i>Cyclol</i> model</a>, the first prediction of the structure of a <a href="/wiki/Globular_protein" title="Globular protein">globular protein</a>.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Contemporary methods are able to determine, without prediction, tertiary structures to within 5 <a href="/wiki/Angstrom" title="Angstrom">Å</a> (0.5 nm) for small proteins (<120 residues) and, under favorable conditions, confident <a href="/wiki/Secondary_structure" class="mw-redirect" title="Secondary structure">secondary structure</a> predictions. </p> <div class="mw-heading mw-heading2"><h2 id="Determinants">Determinants</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=2" title="Edit section: Determinants"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Protein_folding" title="Protein folding">Protein folding</a></div> <div class="mw-heading mw-heading3"><h3 id="Stability_of_native_states">Stability of native states</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=3" title="Edit section: Stability of native states"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading4"><h4 id="Thermostability">Thermostability</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=4" title="Edit section: Thermostability"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">See also: <a href="/wiki/Equilibrium_unfolding" title="Equilibrium unfolding">Equilibrium unfolding</a></div> <p>A protein folded into its <a href="/wiki/Native_state" title="Native state">native state</a> or <a href="/wiki/Chemical_conformation" class="mw-redirect" title="Chemical conformation">native conformation</a> typically has a lower <a href="/wiki/Gibbs_free_energy" title="Gibbs free energy">Gibbs free energy</a> (a combination of <a href="/wiki/Enthalpy" title="Enthalpy">enthalpy</a> and <a href="/wiki/Entropy" title="Entropy">entropy</a>) than the unfolded conformation. A protein will tend towards low-energy conformations, which will determine the protein's fold in the <a href="/wiki/Cell_(biology)" title="Cell (biology)">cellular</a> environment. Because many similar conformations will have similar energies, protein structures are <a href="/wiki/Protein_dynamics" title="Protein dynamics">dynamic</a>, fluctuating between these similar structures. </p><p><a href="/wiki/Globular_protein" title="Globular protein">Globular proteins</a> have a core of <a href="/wiki/Hydrophobic" class="mw-redirect" title="Hydrophobic">hydrophobic</a> amino acid residues and a surface region of <a href="/wiki/Water" title="Water">water</a>-exposed, charged, <a href="/wiki/Hydrophilic" class="mw-redirect" title="Hydrophilic">hydrophilic</a> residues. This arrangement may stabilize interactions within the tertiary structure. For example, in <a href="/wiki/Secrete" class="mw-redirect" title="Secrete">secreted</a> proteins, which are not bathed in <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a>, <a href="/wiki/Disulfide_bond" class="mw-redirect" title="Disulfide bond">disulfide bonds</a> between <a href="/wiki/Cysteine" title="Cysteine">cysteine</a> residues help to maintain the tertiary structure. There is a commonality of stable tertiary structures seen in proteins of diverse function and diverse <a href="/wiki/Molecular_evolution" title="Molecular evolution">evolution</a>. For example, the <a href="/wiki/TIM_barrel" title="TIM barrel">TIM barrel</a>, named for the enzyme <a href="/wiki/Triosephosphateisomerase" class="mw-redirect" title="Triosephosphateisomerase">triosephosphateisomerase</a>, is a common tertiary structure as is the highly stable, <a href="/wiki/Dimer_(chemistry)" class="mw-redirect" title="Dimer (chemistry)">dimeric</a>, <a href="/wiki/Coiled_coil" title="Coiled coil">coiled coil</a> structure. Hence, proteins may be classified by the structures they hold. Databases of proteins which use such a classification include <i><a href="/wiki/Structural_Classification_of_Proteins" class="mw-redirect" title="Structural Classification of Proteins">SCOP</a></i> and <i><a href="/wiki/CATH" class="mw-redirect" title="CATH">CATH</a></i>. </p> <div class="mw-heading mw-heading4"><h4 id="Kinetic_traps">Kinetic traps</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=5" title="Edit section: Kinetic traps"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Folding <a href="/wiki/Chemical_kinetics" title="Chemical kinetics">kinetics</a> may trap a protein in a high-<a href="/wiki/Energy" title="Energy">energy</a> conformation, i.e. a high-energy intermediate conformation blocks access to the lowest-energy conformation. The high-energy conformation may contribute to the function of the protein. For example, the <a href="/wiki/Influenza" title="Influenza">influenza</a> <a href="/wiki/Hemagglutinin" title="Hemagglutinin">hemagglutinin</a> protein is a single polypeptide chain which when activated, is <a href="/wiki/Proteolysis" title="Proteolysis">proteolytically</a> cleaved to form two polypeptide chains. The two chains are held in a high-energy conformation. When the local <a href="/wiki/PH" title="PH">pH</a> drops, the protein undergoes an energetically favorable conformational rearrangement that enables it to penetrate the host <a href="/wiki/Cell_membrane" title="Cell membrane">cell membrane</a>. </p> <div class="mw-heading mw-heading4"><h4 id="Metastability">Metastability</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=6" title="Edit section: Metastability"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Some tertiary protein structures may exist in long-lived states that are not the expected most stable state. For example, many <a href="/wiki/Serpins" class="mw-redirect" title="Serpins">serpins</a> (serine protease inhibitors) show this <a href="/wiki/Metastability" title="Metastability">metastability</a>. They undergo a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a> when a loop of the protein is cut by a <a href="/wiki/Protease" title="Protease">protease</a>.<sup id="cite_ref-whis_5-0" class="reference"><a href="#cite_note-whis-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Chaperone_proteins">Chaperone proteins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=7" title="Edit section: Chaperone proteins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>It is commonly assumed that the native state of a protein is also the most <a href="/wiki/Thermodynamics" title="Thermodynamics">thermodynamically</a> stable and that a protein will reach its native state, given its <a href="/wiki/Chemical_kinetics" title="Chemical kinetics">chemical kinetics</a>, before it is <a href="/wiki/Translation_(genetics)" class="mw-redirect" title="Translation (genetics)">translated</a>. Protein <a href="/wiki/Chaperone_(protein)" title="Chaperone (protein)">chaperones</a> within the cytoplasm of a cell assist a newly synthesised polypeptide to attain its native state. Some chaperone proteins are highly specific in their function, for example, <a href="/wiki/Protein_disulfide_isomerase" class="mw-redirect" title="Protein disulfide isomerase">protein disulfide isomerase</a>; others are general in their function and may assist most globular proteins, for example, the <a href="/wiki/Prokaryotic" class="mw-redirect" title="Prokaryotic">prokaryotic</a> <a href="/wiki/GroEL" title="GroEL">GroEL</a>/<a href="/wiki/GroES" title="GroES">GroES</a> system of proteins and the <a href="/wiki/Homology_(biology)" title="Homology (biology)">homologous</a> <a href="/wiki/Eukaryotic" class="mw-redirect" title="Eukaryotic">eukaryotic</a> <a href="/wiki/Heat_shock_protein" title="Heat shock protein">heat shock proteins</a> (the Hsp60/Hsp10 system). </p> <div class="mw-heading mw-heading3"><h3 id="Cytoplasmic_environment">Cytoplasmic environment</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=8" title="Edit section: Cytoplasmic environment"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Prediction of protein tertiary structure relies on knowing the protein's <a href="/wiki/Primary_structure" class="mw-redirect" title="Primary structure">primary structure</a> and comparing the possible predicted tertiary structure with known tertiary structures in <a href="/wiki/Protein_data_bank" class="mw-redirect" title="Protein data bank">protein data banks</a>. This only takes into account the cytoplasmic environment present at the time of <a href="/wiki/Protein_biosynthesis" title="Protein biosynthesis">protein synthesis</a> to the extent that a similar cytoplasmic environment may also have influenced the structure of the proteins recorded in the protein data bank. </p> <div class="mw-heading mw-heading3"><h3 id="Ligand_binding">Ligand binding</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=9" title="Edit section: Ligand binding"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The structure of a protein, such as an <a href="/wiki/Enzyme" title="Enzyme">enzyme</a>, may change upon binding of its natural ligands, for example a <a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">cofactor</a>. In this case, the structure of the protein bound to the ligand is known as holo structure, while the unbound protein has an apo structure.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p><p>Structure stabilized by the formation of weak bonds between amino acid side chains - Determined by the folding of the polypeptide chain on itself (nonpolar residues are located inside the protein, while polar residues are mainly located outside) - Envelopment of the protein brings the protein closer and relates a-to located in distant regions of the sequence - Acquisition of the tertiary structure leads to the formation of pockets and sites suitable for the recognition and the binding of specific molecules (biospecificity). </p> <div class="mw-heading mw-heading2"><h2 id="Determination">Determination</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=10" title="Edit section: Determination"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The knowledge of the tertiary structure of soluble <a href="/wiki/Globular_protein" title="Globular protein">globular proteins</a> is more advanced than that of <a href="/wiki/Membrane_protein" title="Membrane protein">membrane proteins</a> because the former are easier to study with available technology. </p> <div class="mw-heading mw-heading3"><h3 id="X-ray_crystallography">X-ray crystallography</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=11" title="Edit section: X-ray crystallography"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a> is the most common tool used to determine <a href="/wiki/Protein_structure" title="Protein structure">protein structure</a>. It provides high resolution of the structure but it does not give information about protein's <a href="/wiki/Protein_dynamics" title="Protein dynamics">conformational flexibility</a>. </p> <div class="mw-heading mw-heading3"><h3 id="NMR">NMR</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=12" title="Edit section: NMR"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Protein_NMR" class="mw-redirect" title="Protein NMR">Protein NMR</a> gives comparatively lower resolution of protein structure. It is limited to smaller proteins. However, it can provide information about conformational changes of a protein in solution. </p> <div class="mw-heading mw-heading3"><h3 id="Cryogenic_electron_microscopy">Cryogenic electron microscopy</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=13" title="Edit section: Cryogenic electron microscopy"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Cryogenic_electron_microscopy" title="Cryogenic electron microscopy">Cryogenic electron microscopy</a> (cryo-EM) can give information about both a protein's tertiary and quaternary structure. It is particularly well-suited to large proteins and <a href="/wiki/Protein_complex" title="Protein complex">symmetrical complexes</a> of <a href="/wiki/Protein_subunit" title="Protein subunit">protein subunits</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Dual_polarisation_interferometry">Dual polarisation interferometry</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=14" title="Edit section: Dual polarisation interferometry"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Dual_polarisation_interferometry" class="mw-redirect" title="Dual polarisation interferometry">Dual polarisation interferometry</a> provides complementary information about surface captured proteins. It assists in determining structure and conformation changes over time. </p> <div class="mw-heading mw-heading2"><h2 id="Projects">Projects</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=15" title="Edit section: Projects"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Prediction_algorithm">Prediction algorithm</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=16" title="Edit section: Prediction algorithm"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Folding@home" title="Folding@home">Folding@home</a> project at the <a href="/wiki/University_of_Pennsylvania" title="University of Pennsylvania">University of Pennsylvania</a> is a <a href="/wiki/Distributed_computing" title="Distributed computing">distributed computing</a> research effort which uses approximately 5 <a href="/wiki/PetaFLOPS" class="mw-redirect" title="PetaFLOPS">petaFLOPS</a> (≈10 x86 petaFLOPS) of available computing. It aims to find an <a href="/wiki/Algorithm" title="Algorithm">algorithm</a> which will consistently predict protein tertiary and quaternary structures given the protein's amino acid sequence and its cellular conditions.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p><p>A list of software for protein tertiary structure prediction can be found at <a href="/wiki/List_of_protein_structure_prediction_software" title="List of protein structure prediction software">List of protein structure prediction software</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Protein_aggregation_diseases">Protein aggregation diseases</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=17" title="Edit section: Protein aggregation diseases"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Protein_aggregation" title="Protein aggregation">Protein aggregation</a> diseases such as <a href="/wiki/Alzheimer%27s_disease" title="Alzheimer's disease">Alzheimer's disease</a> and <a href="/wiki/Huntington%27s_disease" title="Huntington's disease">Huntington's disease</a> and <a href="/wiki/Prion" title="Prion">prion</a> diseases such as <a href="/wiki/Bovine_spongiform_encephalopathy" title="Bovine spongiform encephalopathy">bovine spongiform encephalopathy</a> can be better understood by constructing (and reconstructing) <a href="/wiki/Disease_model" class="mw-redirect" title="Disease model">disease models</a>. This is done by causing the disease in laboratory animals, for example, by administering a <a href="/wiki/Toxin" title="Toxin">toxin</a>, such as <a href="/wiki/MPTP" title="MPTP">MPTP</a> to cause Parkinson's disease, or through <a href="/wiki/Genetic_engineering" title="Genetic engineering">genetic manipulation</a>.<sup id="cite_ref-park_11-0" class="reference"><a href="#cite_note-park-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-ko_12-0" class="reference"><a href="#cite_note-ko-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Protein_structure_prediction" title="Protein structure prediction">Protein structure prediction</a> is a new way to create disease models, which may avoid the use of animals.<sup id="cite_ref-bit_13-0" class="reference"><a href="#cite_note-bit-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Protein_Tertiary_Structure_Retrieval_Project_(CoMOGrad)"><span id="Protein_Tertiary_Structure_Retrieval_Project_.28CoMOGrad.29"></span>Protein Tertiary Structure Retrieval Project (CoMOGrad)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=18" title="Edit section: Protein Tertiary Structure Retrieval Project (CoMOGrad)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Matching patterns in tertiary structure of a given protein to huge number of known protein tertiary structures and retrieve most similar ones in ranked order is in the heart of many research areas like function prediction of novel proteins, study of evolution, disease diagnosis, drug discovery, antibody design etc. The CoMOGrad project at BUET is a research effort to device an extremely fast and much precise method for protein tertiary structure retrieval and develop online tool based on research outcome.<sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=19" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1184024115">.mw-parser-output .div-col{margin-top:0.3em;column-width:30em}.mw-parser-output .div-col-small{font-size:90%}.mw-parser-output .div-col-rules{column-rule:1px solid #aaa}.mw-parser-output .div-col dl,.mw-parser-output .div-col ol,.mw-parser-output .div-col ul{margin-top:0}.mw-parser-output .div-col li,.mw-parser-output .div-col dd{page-break-inside:avoid;break-inside:avoid-column}</style><div class="div-col"> <ul><li><a href="/wiki/Folding_(chemistry)" title="Folding (chemistry)">Folding (chemistry)</a></li> <li><a href="/wiki/I-TASSER" title="I-TASSER">I-TASSER</a></li> <li><a href="/wiki/Nucleic_acid_tertiary_structure" title="Nucleic acid tertiary structure">Nucleic acid tertiary structure</a></li> <li><a href="/wiki/Protein_contact_map" title="Protein contact map">Protein contact map</a></li> <li><a href="/wiki/Proteopedia" title="Proteopedia">Proteopedia</a></li> <li><a href="/wiki/Structural_biology" title="Structural biology">Structural biology</a></li> <li><a href="/wiki/Structural_motif" title="Structural motif">Structural motif</a></li> <li><a href="/wiki/Protein_tandem_repeats" title="Protein tandem repeats">Protein tandem repeats</a></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=20" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><a href="/wiki/International_Union_of_Pure_and_Applied_Chemistry" title="International Union of Pure and Applied Chemistry">IUPAC</a>, <i><a href="/wiki/IUPAC_books#Gold_Book" class="mw-redirect" title="IUPAC books">Compendium of Chemical Terminology</a></i>, 2nd ed. (the "Gold Book") (1997). 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title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Scientific+Reports&rft.atitle=CoMOGrad+and+PHOG%3A+From+Computer+Vision+to+Fast+and+Accurate+Protein+Tertiary+Structure+Retrieval&rft.volume=5&rft.issue=1&rft.pages=13275&rft.date=2015-08-21&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4543952%23id-name%3DPMC&rft_id=info%3Abibcode%2F2015NatSR...513275K&rft_id=info%3Aarxiv%2F1409.0814&rft_id=info%3Apmid%2F26293226&rft_id=info%3Adoi%2F10.1038%2Fsrep13275&rft.aulast=Karim&rft.aufirst=Rezaul&rft.au=Aziz%2C+Mohd+Momin+Al&rft.au=Shatabda%2C+Swakkhar&rft.au=Rahman%2C+M.+Sohel&rft.au=Mia%2C+Md+Abul+Kashem&rft.au=Zaman%2C+Farhana&rft.au=Rakin%2C+Salman&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4543952&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein+tertiary+structure" class="Z3988"></span></span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Protein_tertiary_structure&action=edit&section=21" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20150407064348/http://www.pdb.org/">Protein Data Bank</a></li> <li><a rel="nofollow" class="external text" href="http://ca.expasy.org/spdbv/">Display, analyse and superimpose protein 3D structures</a></li> <li><a rel="nofollow" class="external text" href="http://www.bioch.ox.ac.uk/howarth/alphabet.htm">Alphabet of protein structures.</a></li> <li><a rel="nofollow" class="external text" href="http://swift.cmbi.ru.nl/whatif/">Display, analyse and superimpose protein 3D structures</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20110718132234/http://swift.cmbi.ru.nl/teach/B1/">WWW-based course teaching elementary protein bioinformatics</a></li> <li><a rel="nofollow" class="external text" href="https://predictioncenter.org/">Critical Assessment of Structure Prediction (CASP)</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20070911012207/http://scop.mrc-lmb.cam.ac.uk/scop/">Structural Classification of Proteins (SCOP)</a></li> <li><a rel="nofollow" class="external text" href="http://www.cathdb.info/">CATH Protein Structure Classification</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20051125045348/http://ekhidna.biocenter.helsinki.fi/dali/start">DALI/FSSP software and database of superposed protein structures</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20081215084435/http://mozart.bio.neu.edu/topofit/index.php">TOPOFIT-DB Invariant Structural Cores between proteins</a></li> <li><a href="/wiki/PDBWiki" title="PDBWiki">PDBWiki</a> — <a rel="nofollow" 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class="mw-selflink selflink">Protein tertiary structure</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">General</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein_domain" title="Protein domain">Structural domain</a></li> <li><a href="/wiki/Protein_folding" title="Protein folding">Protein folding</a></li> <li><a href="/wiki/Protein_structure" title="Protein structure">Structure determination methods</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">All-α folds:</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Helix_bundle" title="Helix bundle">Helix bundle</a></li> <li><a href="/wiki/Globin_fold" class="mw-redirect" title="Globin fold">Globin fold</a></li> <li><a href="/wiki/Homeodomain_fold" class="mw-redirect" title="Homeodomain fold">Homeodomain fold</a></li> <li><a href="/wiki/Alpha_solenoid" title="Alpha solenoid">Alpha solenoid</a></li> <li><a href="/wiki/Death_fold" title="Death fold">Death fold</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">All-β folds:</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Immunoglobulin_domain" title="Immunoglobulin domain">Immunoglobulin domain</a></li> <li><a href="/wiki/Beta_barrel" title="Beta barrel">Beta barrel</a></li> <li><a href="/wiki/Beta-propeller" title="Beta-propeller">Beta-propeller</a></li> <li><a href="/wiki/Beta_helix" title="Beta helix">Beta helix</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">α/β folds:</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/TIM_barrel" title="TIM barrel">TIM barrel</a></li> <li><a href="/wiki/Leucine-rich_repeat" title="Leucine-rich repeat">Leucine-rich repeat</a></li> <li><a href="/wiki/Flavodoxin_fold" title="Flavodoxin fold">Flavodoxin fold</a></li> <li><a href="/wiki/Rossmann_fold" title="Rossmann fold">Rossmann fold</a></li> <li><a href="/wiki/Thioredoxin_fold" title="Thioredoxin fold">Thioredoxin fold</a></li> <li><a href="/wiki/Trefoil_knot_fold" title="Trefoil knot fold">Trefoil knot fold</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">α+β folds:</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/DNA_clamp" title="DNA clamp">DNA clamp</a></li> <li><a href="/wiki/Ferredoxin_fold" title="Ferredoxin fold">Ferredoxin fold</a></li> <li><a href="/wiki/Ribonuclease_A" class="mw-redirect" title="Ribonuclease A">Ribonuclease A</a></li> <li><a href="/wiki/SH2_domain" title="SH2 domain">SH2-like fold</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Irregular folds:</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Conotoxin" title="Conotoxin">Conotoxin</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Biomolecular_structure" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2" style="background:lightblue"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Biomolecular_structure" title="Template:Biomolecular structure"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Biomolecular_structure" title="Template talk:Biomolecular structure"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Biomolecular_structure" title="Special:EditPage/Template:Biomolecular structure"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Biomolecular_structure" style="font-size:114%;margin:0 4em"><a href="/wiki/Biomolecular_structure" title="Biomolecular structure">Biomolecular structure</a></div></th></tr><tr><th scope="row" class="navbox-group" style="background:lightblue;width:1%"><a href="/wiki/Protein_structure" title="Protein structure">Protein</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein_primary_structure" title="Protein primary structure">Primary</a></li> <li><a href="/wiki/Protein_secondary_structure" title="Protein secondary structure">Secondary</a></li> <li><a class="mw-selflink selflink">Tertiary</a></li> <li><a href="/wiki/Protein_quaternary_structure" title="Protein quaternary structure">Quaternary</a></li> <li><a href="/wiki/Protein_structure#Protein_structure_determination" title="Protein structure">Determination</a></li> <li><a href="/wiki/Protein_structure_prediction" title="Protein structure prediction">Prediction</a></li> <li><a href="/wiki/Protein_design" title="Protein design">Design</a></li> <li><a href="/wiki/Protein_thermodynamics" class="mw-redirect" title="Protein thermodynamics">Thermodynamics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="background:lightblue;width:1%"><a href="/wiki/Nucleic_acid_structure" title="Nucleic acid structure">Nucleic acid</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Nucleic_acid_sequence" title="Nucleic acid sequence">Primary</a></li> <li><a href="/wiki/Nucleic_acid_secondary_structure" title="Nucleic acid secondary structure">Secondary</a></li> <li><a href="/wiki/Nucleic_acid_tertiary_structure" title="Nucleic acid tertiary structure">Tertiary</a></li> <li><a href="/wiki/Nucleic_acid_quaternary_structure" title="Nucleic acid quaternary structure">Quaternary</a></li> <li><a href="/wiki/Nucleic_acid_structure_determination" title="Nucleic acid structure determination">Determination</a></li> <li><a href="/wiki/Nucleic_acid_structure_prediction" title="Nucleic acid structure prediction">Prediction</a></li> <li><a href="/wiki/Nucleic_acid_design" title="Nucleic acid design">Design</a></li> <li><a href="/wiki/Nucleic_acid_thermodynamics" title="Nucleic acid thermodynamics">Thermodynamics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="background:lightblue;width:1%">See also</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein" title="Protein">Protein</a></li> <li><a href="/wiki/Protein_domain" title="Protein domain">Protein domain</a></li> <li><a href="/wiki/Protein_engineering" title="Protein engineering">Protein engineering</a></li> <li><a href="/wiki/Proteasome" title="Proteasome">Proteasome</a></li> <li><a href="/wiki/Nucleic_acid" title="Nucleic acid">Nucleic acid</a></li> <li><a href="/wiki/DNA" title="DNA">DNA</a></li> <li><a href="/wiki/RNA" title="RNA">RNA</a></li> <li><a href="/wiki/Structural_motif" title="Structural motif">Structural motif</a></li> <li><a href="/wiki/Nucleic_acid_double_helix" title="Nucleic acid double helix">Nucleic acid double helix</a></li></ul> </div></td></tr></tbody></table></div> <!-- NewPP limit report Parsed by mw‐web.codfw.main‐f69cdc8f6‐ffqzr Cached time: 20241122140845 Cache expiry: 2592000 Reduced expiry: false Complications: [vary‐revision‐sha1, show‐toc] CPU time usage: 0.463 seconds Real time usage: 0.680 seconds Preprocessor visited node count: 1712/1000000 Post‐expand include size: 53045/2097152 bytes Template argument size: 1016/2097152 bytes Highest expansion depth: 16/100 Expensive parser function count: 5/500 Unstrip recursion depth: 1/20 Unstrip post‐expand size: 72144/5000000 bytes Lua time usage: 0.277/10.000 seconds Lua memory usage: 6163003/52428800 bytes Number of Wikibase entities loaded: 0/400 --> <!-- Transclusion expansion time report (%,ms,calls,template) 100.00% 598.406 1 -total 33.14% 198.293 1 Template:Reflist 23.36% 139.815 1 Template:Short_description 18.53% 110.887 2 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