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class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Classification" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Classification"> <div class="vector-toc-text"> <span class="vector-toc-numb">2</span> <span>Classification</span> </div> </a> <ul id="toc-Classification-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Biochemistry" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Biochemistry"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Biochemistry</span> </div> </a> <button aria-controls="toc-Biochemistry-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 Biochemistry subsection</span> </button> <ul id="toc-Biochemistry-sublist" class="vector-toc-list"> <li id="toc-Abundance_in_cells" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Abundance_in_cells"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.1</span> <span>Abundance in cells</span> </div> </a> <ul id="toc-Abundance_in_cells-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Synthesis" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Synthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Synthesis</span> </div> </a> <button aria-controls="toc-Synthesis-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 Synthesis subsection</span> </button> <ul id="toc-Synthesis-sublist" class="vector-toc-list"> <li id="toc-Biosynthesis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Biosynthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Biosynthesis</span> </div> </a> <ul id="toc-Biosynthesis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chemical_synthesis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chemical_synthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Chemical synthesis</span> </div> </a> <ul id="toc-Chemical_synthesis-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Structure_2" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Structure_2"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Structure</span> </div> </a> <button aria-controls="toc-Structure_2-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 Structure subsection</span> </button> <ul id="toc-Structure_2-sublist" class="vector-toc-list"> <li id="toc-Protein_domains" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Protein_domains"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.1</span> <span>Protein domains</span> </div> </a> <ul id="toc-Protein_domains-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Sequence_motif" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Sequence_motif"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.2</span> <span>Sequence motif</span> </div> </a> <ul id="toc-Sequence_motif-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Cellular_functions" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Cellular_functions"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Cellular functions</span> </div> </a> <button aria-controls="toc-Cellular_functions-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 Cellular functions subsection</span> </button> <ul id="toc-Cellular_functions-sublist" class="vector-toc-list"> <li id="toc-Enzymes" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Enzymes"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.1</span> <span>Enzymes</span> </div> </a> <ul id="toc-Enzymes-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cell_signaling_and_ligand_binding" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cell_signaling_and_ligand_binding"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.2</span> <span>Cell signaling and ligand binding</span> </div> </a> <ul id="toc-Cell_signaling_and_ligand_binding-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Structural_proteins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Structural_proteins"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.3</span> <span>Structural proteins</span> </div> </a> <ul id="toc-Structural_proteins-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Methods_of_study" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Methods_of_study"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Methods of study</span> </div> </a> <button aria-controls="toc-Methods_of_study-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 Methods of study subsection</span> </button> <ul id="toc-Methods_of_study-sublist" class="vector-toc-list"> <li id="toc-Protein_purification" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Protein_purification"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.1</span> <span>Protein purification</span> </div> </a> <ul id="toc-Protein_purification-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cellular_localization" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cellular_localization"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2</span> <span>Cellular localization</span> </div> </a> <ul id="toc-Cellular_localization-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Proteomics" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Proteomics"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.3</span> <span>Proteomics</span> </div> </a> <ul id="toc-Proteomics-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Structure_determination" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Structure_determination"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.4</span> <span>Structure determination</span> </div> </a> <ul id="toc-Structure_determination-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Structure_prediction" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Structure_prediction"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.5</span> <span>Structure prediction</span> </div> </a> <ul id="toc-Structure_prediction-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-In_silico_simulation_of_dynamical_processes" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#In_silico_simulation_of_dynamical_processes"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.6</span> <span>In silico simulation of dynamical processes</span> </div> </a> <ul id="toc-In_silico_simulation_of_dynamical_processes-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chemical_analysis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chemical_analysis"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.7</span> <span>Chemical analysis</span> </div> </a> <ul id="toc-Chemical_analysis-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Digestion" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Digestion"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Digestion</span> </div> </a> <ul id="toc-Digestion-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Mechanical_properties" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Mechanical_properties"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>Mechanical properties</span> </div> </a> <ul id="toc-Mechanical_properties-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</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"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">11</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Further_reading" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Further_reading"> <div class="vector-toc-text"> <span class="vector-toc-numb">12</span> <span>Further reading</span> </div> </a> <ul id="toc-Further_reading-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">13</span> <span>External links</span> </div> </a> <button aria-controls="toc-External_links-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 External links subsection</span> </button> <ul id="toc-External_links-sublist" class="vector-toc-list"> <li id="toc-Databases_and_projects" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Databases_and_projects"> <div class="vector-toc-text"> <span class="vector-toc-numb">13.1</span> <span>Databases and projects</span> </div> </a> <ul id="toc-Databases_and_projects-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Tutorials_and_educational_websites" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Tutorials_and_educational_websites"> <div class="vector-toc-text"> <span class="vector-toc-numb">13.2</span> <span>Tutorials and educational websites</span> </div> </a> <ul id="toc-Tutorials_and_educational_websites-sublist" class="vector-toc-list"> </ul> </li> </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" title="Table of Contents" > <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</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 163 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-163" 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">163 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-af mw-list-item"><a href="https://af.wikipedia.org/wiki/Prote%C3%AFen" title="Proteïen – Afrikaans" lang="af" hreflang="af" data-title="Proteïen" data-language-autonym="Afrikaans" data-language-local-name="Afrikaans" class="interlanguage-link-target"><span>Afrikaans</span></a></li><li class="interlanguage-link interwiki-als mw-list-item"><a href="https://als.wikipedia.org/wiki/Protein" title="Protein – Alemannic" lang="gsw" hreflang="gsw" data-title="Protein" data-language-autonym="Alemannisch" data-language-local-name="Alemannic" class="interlanguage-link-target"><span>Alemannisch</span></a></li><li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D8%A8%D8%B1%D9%88%D8%AA%D9%8A%D9%86" title="بروتين – Arabic" lang="ar" hreflang="ar" data-title="بروتين" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-an mw-list-item"><a href="https://an.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Aragonese" lang="an" hreflang="an" data-title="Proteína" data-language-autonym="Aragonés" data-language-local-name="Aragonese" class="interlanguage-link-target"><span>Aragonés</span></a></li><li class="interlanguage-link interwiki-as mw-list-item"><a href="https://as.wikipedia.org/wiki/%E0%A6%AE%E0%A6%BE%E0%A6%82%E0%A6%B8%E0%A6%B8%E0%A6%BE%E0%A7%B0" title="মাংসসাৰ – Assamese" lang="as" hreflang="as" data-title="মাংসসাৰ" data-language-autonym="অসমীয়া" data-language-local-name="Assamese" class="interlanguage-link-target"><span>অসমীয়া</span></a></li><li class="interlanguage-link interwiki-ast mw-list-item"><a href="https://ast.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Asturian" lang="ast" hreflang="ast" data-title="Proteína" data-language-autonym="Asturianu" data-language-local-name="Asturian" class="interlanguage-link-target"><span>Asturianu</span></a></li><li class="interlanguage-link interwiki-gn mw-list-item"><a href="https://gn.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Guarani" lang="gn" hreflang="gn" data-title="Proteína" data-language-autonym="Avañe'ẽ" data-language-local-name="Guarani" class="interlanguage-link-target"><span>Avañe'ẽ</span></a></li><li class="interlanguage-link interwiki-az mw-list-item"><a href="https://az.wikipedia.org/wiki/Z%C3%BClallar" title="Zülallar – Azerbaijani" lang="az" hreflang="az" data-title="Zülallar" data-language-autonym="Azərbaycanca" data-language-local-name="Azerbaijani" class="interlanguage-link-target"><span>Azərbaycanca</span></a></li><li class="interlanguage-link interwiki-azb mw-list-item"><a href="https://azb.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D8%AA%D8%A6%DB%8C%D9%86" title="پروتئین – South Azerbaijani" lang="azb" hreflang="azb" data-title="پروتئین" data-language-autonym="تۆرکجه" data-language-local-name="South Azerbaijani" class="interlanguage-link-target"><span>تۆرکجه</span></a></li><li class="interlanguage-link interwiki-ban mw-list-item"><a href="https://ban.wikipedia.org/wiki/Prot%C3%A9in" title="Protéin – Balinese" lang="ban" hreflang="ban" data-title="Protéin" data-language-autonym="Basa Bali" data-language-local-name="Balinese" class="interlanguage-link-target"><span>Basa Bali</span></a></li><li class="interlanguage-link interwiki-bn mw-list-item"><a href="https://bn.wikipedia.org/wiki/%E0%A6%AA%E0%A7%8D%E0%A6%B0%E0%A7%8B%E0%A6%9F%E0%A6%BF%E0%A6%A8" title="প্রোটিন – Bangla" lang="bn" hreflang="bn" data-title="প্রোটিন" data-language-autonym="বাংলা" data-language-local-name="Bangla" class="interlanguage-link-target"><span>বাংলা</span></a></li><li class="interlanguage-link interwiki-bjn mw-list-item"><a href="https://bjn.wikipedia.org/wiki/Parot%C3%A9in" title="Parotéin – Banjar" lang="bjn" hreflang="bjn" data-title="Parotéin" data-language-autonym="Banjar" data-language-local-name="Banjar" class="interlanguage-link-target"><span>Banjar</span></a></li><li class="interlanguage-link interwiki-zh-min-nan mw-list-item"><a href="https://zh-min-nan.wikipedia.org/wiki/Nn%CC%84g-pe%CC%8Dh-chit" title="Nn̄g-pe̍h-chit – Minnan" lang="nan" hreflang="nan" data-title="Nn̄g-pe̍h-chit" data-language-autonym="閩南語 / Bân-lâm-gú" data-language-local-name="Minnan" class="interlanguage-link-target"><span>閩南語 / Bân-lâm-gú</span></a></li><li class="interlanguage-link interwiki-ba mw-list-item"><a href="https://ba.wikipedia.org/wiki/%D0%90%D2%A1%D2%BB%D1%8B%D0%BC%D0%B4%D0%B0%D1%80" title="Аҡһымдар – Bashkir" lang="ba" hreflang="ba" data-title="Аҡһымдар" data-language-autonym="Башҡортса" data-language-local-name="Bashkir" class="interlanguage-link-target"><span>Башҡортса</span></a></li><li class="interlanguage-link interwiki-be mw-list-item"><a href="https://be.wikipedia.org/wiki/%D0%91%D1%8F%D0%BB%D0%BA%D1%96" title="Бялкі – Belarusian" lang="be" hreflang="be" data-title="Бялкі" data-language-autonym="Беларуская" data-language-local-name="Belarusian" class="interlanguage-link-target"><span>Беларуская</span></a></li><li class="interlanguage-link interwiki-be-x-old mw-list-item"><a href="https://be-tarask.wikipedia.org/wiki/%D0%91%D1%8F%D0%BB%D0%BA%D1%96" title="Бялкі – Belarusian (Taraškievica orthography)" lang="be-tarask" hreflang="be-tarask" data-title="Бялкі" data-language-autonym="Беларуская (тарашкевіца)" data-language-local-name="Belarusian (Taraškievica orthography)" class="interlanguage-link-target"><span>Беларуская (тарашкевіца)</span></a></li><li class="interlanguage-link interwiki-bh mw-list-item"><a href="https://bh.wikipedia.org/wiki/%E0%A4%AA%E0%A5%8D%E0%A4%B0%E0%A5%8B%E0%A4%9F%E0%A5%80%E0%A4%A8" title="प्रोटीन – Bhojpuri" lang="bh" hreflang="bh" data-title="प्रोटीन" data-language-autonym="भोजपुरी" data-language-local-name="Bhojpuri" class="interlanguage-link-target"><span>भोजपुरी</span></a></li><li class="interlanguage-link interwiki-bcl mw-list-item"><a href="https://bcl.wikipedia.org/wiki/Protina" title="Protina – Central Bikol" lang="bcl" hreflang="bcl" data-title="Protina" data-language-autonym="Bikol Central" data-language-local-name="Central Bikol" class="interlanguage-link-target"><span>Bikol Central</span></a></li><li class="interlanguage-link interwiki-bg mw-list-item"><a href="https://bg.wikipedia.org/wiki/%D0%9F%D1%80%D0%BE%D1%82%D0%B5%D0%B8%D0%BD" title="Протеин – Bulgarian" lang="bg" hreflang="bg" data-title="Протеин" data-language-autonym="Български" data-language-local-name="Bulgarian" class="interlanguage-link-target"><span>Български</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Bjelan%C4%8Devine" title="Bjelančevine – Bosnian" lang="bs" hreflang="bs" data-title="Bjelančevine" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-br mw-list-item"><a href="https://br.wikipedia.org/wiki/Protein" title="Protein – Breton" lang="br" hreflang="br" data-title="Protein" data-language-autonym="Brezhoneg" data-language-local-name="Breton" class="interlanguage-link-target"><span>Brezhoneg</span></a></li><li class="interlanguage-link interwiki-bxr mw-list-item"><a href="https://bxr.wikipedia.org/wiki/%D0%A3%D1%83%D1%80%D0%B0%D0%B3" title="Уураг – Russia Buriat" lang="bxr" hreflang="bxr" data-title="Уураг" data-language-autonym="Буряад" data-language-local-name="Russia Buriat" class="interlanguage-link-target"><span>Буряад</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Prote%C3%AFna" title="Proteïna – Catalan" lang="ca" hreflang="ca" data-title="Proteïna" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-cv mw-list-item"><a href="https://cv.wikipedia.org/wiki/%D0%A8%D1%83%D1%80%D1%80%D0%B8" title="Шурри – Chuvash" lang="cv" hreflang="cv" data-title="Шурри" data-language-autonym="Чӑвашла" data-language-local-name="Chuvash" class="interlanguage-link-target"><span>Чӑвашла</span></a></li><li class="interlanguage-link interwiki-ceb mw-list-item"><a href="https://ceb.wikipedia.org/wiki/Protina_(kimika)" title="Protina (kimika) – Cebuano" lang="ceb" hreflang="ceb" data-title="Protina (kimika)" data-language-autonym="Cebuano" data-language-local-name="Cebuano" class="interlanguage-link-target"><span>Cebuano</span></a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/B%C3%ADlkovina" title="Bílkovina – Czech" lang="cs" hreflang="cs" data-title="Bílkovina" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target"><span>Čeština</span></a></li><li class="interlanguage-link interwiki-cy mw-list-item"><a href="https://cy.wikipedia.org/wiki/Protein" title="Protein – Welsh" lang="cy" hreflang="cy" data-title="Protein" data-language-autonym="Cymraeg" data-language-local-name="Welsh" class="interlanguage-link-target"><span>Cymraeg</span></a></li><li class="interlanguage-link interwiki-da mw-list-item"><a href="https://da.wikipedia.org/wiki/Protein" title="Protein – Danish" lang="da" hreflang="da" data-title="Protein" data-language-autonym="Dansk" data-language-local-name="Danish" class="interlanguage-link-target"><span>Dansk</span></a></li><li class="interlanguage-link interwiki-ary mw-list-item"><a href="https://ary.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D8%AA%D9%8A%D9%86" title="پروتين – Moroccan Arabic" lang="ary" hreflang="ary" data-title="پروتين" data-language-autonym="الدارجة" data-language-local-name="Moroccan Arabic" class="interlanguage-link-target"><span>الدارجة</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Protein" title="Protein – German" lang="de" hreflang="de" data-title="Protein" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-dv mw-list-item"><a href="https://dv.wikipedia.org/wiki/%DE%95%DE%B0%DE%83%DE%AE%DE%93%DE%A9%DE%82%DE%B0" title="ޕްރޮޓީން – Divehi" lang="dv" hreflang="dv" data-title="ޕްރޮޓީން" data-language-autonym="ދިވެހިބަސް" data-language-local-name="Divehi" class="interlanguage-link-target"><span>ދިވެހިބަސް</span></a></li><li class="interlanguage-link interwiki-dty mw-list-item"><a href="https://dty.wikipedia.org/wiki/%E0%A4%AA%E0%A5%8D%E0%A4%B0%E0%A5%8B%E0%A4%9F%E0%A4%BF%E0%A4%A8" title="प्रोटिन – Doteli" lang="dty" hreflang="dty" data-title="प्रोटिन" data-language-autonym="डोटेली" data-language-local-name="Doteli" class="interlanguage-link-target"><span>डोटेली</span></a></li><li class="interlanguage-link interwiki-et mw-list-item"><a href="https://et.wikipedia.org/wiki/Valgud" title="Valgud – Estonian" lang="et" hreflang="et" data-title="Valgud" data-language-autonym="Eesti" data-language-local-name="Estonian" class="interlanguage-link-target"><span>Eesti</span></a></li><li class="interlanguage-link interwiki-el mw-list-item"><a href="https://el.wikipedia.org/wiki/%CE%A0%CF%81%CF%89%CF%84%CE%B5%CE%90%CE%BD%CE%B7" title="Πρωτεΐνη – Greek" lang="el" hreflang="el" data-title="Πρωτεΐνη" data-language-autonym="Ελληνικά" data-language-local-name="Greek" class="interlanguage-link-target"><span>Ελληνικά</span></a></li><li class="interlanguage-link interwiki-myv mw-list-item"><a href="https://myv.wikipedia.org/wiki/%D0%90%D1%88%D0%BE%D0%B2%D1%82" title="Ашовт – Erzya" lang="myv" hreflang="myv" data-title="Ашовт" data-language-autonym="Эрзянь" data-language-local-name="Erzya" class="interlanguage-link-target"><span>Эрзянь</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Spanish" lang="es" hreflang="es" data-title="Proteína" 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/Proteino" title="Proteino – Esperanto" lang="eo" hreflang="eo" data-title="Proteino" data-language-autonym="Esperanto" data-language-local-name="Esperanto" class="interlanguage-link-target"><span>Esperanto</span></a></li><li class="interlanguage-link interwiki-ext mw-list-item"><a href="https://ext.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Extremaduran" lang="ext" hreflang="ext" data-title="Proteína" data-language-autonym="Estremeñu" data-language-local-name="Extremaduran" class="interlanguage-link-target"><span>Estremeñu</span></a></li><li class="interlanguage-link interwiki-eu mw-list-item"><a href="https://eu.wikipedia.org/wiki/Proteina" title="Proteina – Basque" lang="eu" hreflang="eu" data-title="Proteina" data-language-autonym="Euskara" data-language-local-name="Basque" class="interlanguage-link-target"><span>Euskara</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D8%AA%D8%A6%DB%8C%D9%86" title="پروتئین – Persian" lang="fa" hreflang="fa" data-title="پروتئین" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-hif mw-list-item"><a href="https://hif.wikipedia.org/wiki/Protein" title="Protein – Fiji Hindi" lang="hif" hreflang="hif" data-title="Protein" data-language-autonym="Fiji Hindi" data-language-local-name="Fiji Hindi" class="interlanguage-link-target"><span>Fiji Hindi</span></a></li><li class="interlanguage-link interwiki-fo mw-list-item"><a href="https://fo.wikipedia.org/wiki/Protein" title="Protein – Faroese" lang="fo" hreflang="fo" data-title="Protein" data-language-autonym="Føroyskt" data-language-local-name="Faroese" class="interlanguage-link-target"><span>Føroyskt</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Prot%C3%A9ine" title="Protéine – French" lang="fr" hreflang="fr" data-title="Protéine" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-fy mw-list-item"><a href="https://fy.wikipedia.org/wiki/Aaiwyt_(stof)" title="Aaiwyt (stof) – Western Frisian" lang="fy" hreflang="fy" data-title="Aaiwyt (stof)" data-language-autonym="Frysk" data-language-local-name="Western Frisian" class="interlanguage-link-target"><span>Frysk</span></a></li><li class="interlanguage-link interwiki-ga mw-list-item"><a href="https://ga.wikipedia.org/wiki/Pr%C3%B3it%C3%A9in" title="Próitéin – Irish" lang="ga" hreflang="ga" data-title="Próitéin" data-language-autonym="Gaeilge" data-language-local-name="Irish" class="interlanguage-link-target"><span>Gaeilge</span></a></li><li class="interlanguage-link interwiki-gv mw-list-item"><a href="https://gv.wikipedia.org/wiki/Proteen" title="Proteen – Manx" lang="gv" hreflang="gv" data-title="Proteen" data-language-autonym="Gaelg" data-language-local-name="Manx" class="interlanguage-link-target"><span>Gaelg</span></a></li><li class="interlanguage-link interwiki-gd mw-list-item"><a href="https://gd.wikipedia.org/wiki/Pr%C3%B2tain" title="Pròtain – Scottish Gaelic" lang="gd" hreflang="gd" data-title="Pròtain" data-language-autonym="Gàidhlig" data-language-local-name="Scottish Gaelic" class="interlanguage-link-target"><span>Gàidhlig</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Galician" lang="gl" hreflang="gl" data-title="Proteína" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-inh mw-list-item"><a href="https://inh.wikipedia.org/wiki/%D0%91%D0%B5%D0%BB%D0%BE%D0%BA%D0%B0%D1%88" title="Белокаш – Ingush" lang="inh" hreflang="inh" data-title="Белокаш" data-language-autonym="ГӀалгӀай" data-language-local-name="Ingush" class="interlanguage-link-target"><span>ГӀалгӀай</span></a></li><li class="interlanguage-link interwiki-hak mw-list-item"><a href="https://hak.wikipedia.org/wiki/Th%C3%A0n-pha%CC%8Dk-ch%E1%B9%B3t" title="Thàn-pha̍k-chṳt – Hakka Chinese" lang="hak" hreflang="hak" data-title="Thàn-pha̍k-chṳt" data-language-autonym="客家語 / Hak-kâ-ngî" data-language-local-name="Hakka Chinese" class="interlanguage-link-target"><span>客家語 / Hak-kâ-ngî</span></a></li><li class="interlanguage-link interwiki-xal mw-list-item"><a href="https://xal.wikipedia.org/wiki/%D0%A3%D1%83%D1%80%D1%83%D0%B3" title="Ууруг – Kalmyk" lang="xal" hreflang="xal" data-title="Ууруг" data-language-autonym="Хальмг" data-language-local-name="Kalmyk" class="interlanguage-link-target"><span>Хальмг</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" title="단백질 – Korean" lang="ko" hreflang="ko" data-title="단백질" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-hy badge-Q17437796 badge-featuredarticle mw-list-item" title="featured article badge"><a href="https://hy.wikipedia.org/wiki/%D5%8D%D5%BA%D5%AB%D5%BF%D5%A1%D5%AF%D5%B8%D6%82%D6%81%D5%B6%D5%A5%D6%80" title="Սպիտակուցներ – Armenian" lang="hy" hreflang="hy" data-title="Սպիտակուցներ" data-language-autonym="Հայերեն" data-language-local-name="Armenian" class="interlanguage-link-target"><span>Հայերեն</span></a></li><li class="interlanguage-link interwiki-hi mw-list-item"><a href="https://hi.wikipedia.org/wiki/%E0%A4%AA%E0%A5%8D%E0%A4%B0%E0%A5%8B%E0%A4%9F%E0%A5%80%E0%A4%A8" title="प्रोटीन – Hindi" lang="hi" hreflang="hi" data-title="प्रोटीन" data-language-autonym="हिन्दी" data-language-local-name="Hindi" class="interlanguage-link-target"><span>हिन्दी</span></a></li><li class="interlanguage-link interwiki-hr mw-list-item"><a href="https://hr.wikipedia.org/wiki/Bjelan%C4%8Devine" title="Bjelančevine – Croatian" lang="hr" hreflang="hr" data-title="Bjelančevine" data-language-autonym="Hrvatski" data-language-local-name="Croatian" class="interlanguage-link-target"><span>Hrvatski</span></a></li><li class="interlanguage-link interwiki-io mw-list-item"><a href="https://io.wikipedia.org/wiki/Proteino" title="Proteino – Ido" lang="io" hreflang="io" data-title="Proteino" data-language-autonym="Ido" data-language-local-name="Ido" class="interlanguage-link-target"><span>Ido</span></a></li><li class="interlanguage-link interwiki-ilo mw-list-item"><a href="https://ilo.wikipedia.org/wiki/Protina" title="Protina – Iloko" lang="ilo" hreflang="ilo" data-title="Protina" data-language-autonym="Ilokano" data-language-local-name="Iloko" class="interlanguage-link-target"><span>Ilokano</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Protein" title="Protein – Indonesian" lang="id" hreflang="id" data-title="Protein" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target"><span>Bahasa Indonesia</span></a></li><li class="interlanguage-link interwiki-ia mw-list-item"><a href="https://ia.wikipedia.org/wiki/Proteina" title="Proteina – Interlingua" lang="ia" hreflang="ia" data-title="Proteina" data-language-autonym="Interlingua" data-language-local-name="Interlingua" class="interlanguage-link-target"><span>Interlingua</span></a></li><li class="interlanguage-link interwiki-zu mw-list-item"><a href="https://zu.wikipedia.org/wiki/Isakhamzimba" title="Isakhamzimba – Zulu" lang="zu" hreflang="zu" data-title="Isakhamzimba" data-language-autonym="IsiZulu" data-language-local-name="Zulu" class="interlanguage-link-target"><span>IsiZulu</span></a></li><li class="interlanguage-link interwiki-is mw-list-item"><a href="https://is.wikipedia.org/wiki/Pr%C3%B3t%C3%ADn" title="Prótín – Icelandic" lang="is" hreflang="is" data-title="Prótín" data-language-autonym="Íslenska" data-language-local-name="Icelandic" class="interlanguage-link-target"><span>Íslenska</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Proteine" title="Proteine – Italian" lang="it" hreflang="it" data-title="Proteine" 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%97%D7%9C%D7%91%D7%95%D7%9F" title="חלבון – Hebrew" lang="he" hreflang="he" data-title="חלבון" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-jv mw-list-item"><a href="https://jv.wikipedia.org/wiki/Prot%C3%A9in" title="Protéin – Javanese" lang="jv" hreflang="jv" data-title="Protéin" data-language-autonym="Jawa" data-language-local-name="Javanese" class="interlanguage-link-target"><span>Jawa</span></a></li><li class="interlanguage-link interwiki-kn mw-list-item"><a href="https://kn.wikipedia.org/wiki/%E0%B2%AA%E0%B3%8D%E0%B2%B0%E0%B3%8B%E0%B2%9F%E0%B3%80%E0%B2%A8%E0%B3%8D" title="ಪ್ರೋಟೀನ್ – Kannada" lang="kn" hreflang="kn" data-title="ಪ್ರೋಟೀನ್" data-language-autonym="ಕನ್ನಡ" data-language-local-name="Kannada" class="interlanguage-link-target"><span>ಕನ್ನಡ</span></a></li><li class="interlanguage-link interwiki-pam mw-list-item"><a href="https://pam.wikipedia.org/wiki/Protina" title="Protina – Pampanga" lang="pam" hreflang="pam" data-title="Protina" data-language-autonym="Kapampangan" data-language-local-name="Pampanga" class="interlanguage-link-target"><span>Kapampangan</span></a></li><li class="interlanguage-link interwiki-ka mw-list-item"><a href="https://ka.wikipedia.org/wiki/%E1%83%AA%E1%83%98%E1%83%9A%E1%83%94%E1%83%91%E1%83%98" title="ცილები – Georgian" lang="ka" hreflang="ka" data-title="ცილები" data-language-autonym="ქართული" data-language-local-name="Georgian" class="interlanguage-link-target"><span>ქართული</span></a></li><li class="interlanguage-link interwiki-ks mw-list-item"><a href="https://ks.wikipedia.org/wiki/%D9%BE%D8%B1%D9%9B%D9%88%D9%B9%DB%8C%D9%96%D9%86" title="پرٛوٹیٖن – Kashmiri" lang="ks" hreflang="ks" data-title="پرٛوٹیٖن" data-language-autonym="कॉशुर / کٲشُر" data-language-local-name="Kashmiri" class="interlanguage-link-target"><span>कॉशुर / کٲشُر</span></a></li><li class="interlanguage-link interwiki-kk mw-list-item"><a href="https://kk.wikipedia.org/wiki/%D0%90%D2%9B%D1%83%D1%8B%D0%B7" title="Ақуыз – Kazakh" lang="kk" hreflang="kk" data-title="Ақуыз" data-language-autonym="Қазақша" data-language-local-name="Kazakh" class="interlanguage-link-target"><span>Қазақша</span></a></li><li class="interlanguage-link interwiki-kw mw-list-item"><a href="https://kw.wikipedia.org/wiki/Protin" title="Protin – Cornish" lang="kw" hreflang="kw" data-title="Protin" data-language-autonym="Kernowek" data-language-local-name="Cornish" class="interlanguage-link-target"><span>Kernowek</span></a></li><li class="interlanguage-link interwiki-sw mw-list-item"><a href="https://sw.wikipedia.org/wiki/Protini" title="Protini – Swahili" lang="sw" hreflang="sw" data-title="Protini" data-language-autonym="Kiswahili" data-language-local-name="Swahili" class="interlanguage-link-target"><span>Kiswahili</span></a></li><li class="interlanguage-link interwiki-ht mw-list-item"><a href="https://ht.wikipedia.org/wiki/Pwoteyin" title="Pwoteyin – Haitian Creole" lang="ht" hreflang="ht" data-title="Pwoteyin" data-language-autonym="Kreyòl ayisyen" data-language-local-name="Haitian Creole" class="interlanguage-link-target"><span>Kreyòl ayisyen</span></a></li><li class="interlanguage-link interwiki-ku mw-list-item"><a href="https://ku.wikipedia.org/wiki/Prote%C3%AEn" title="Proteîn – Kurdish" lang="ku" hreflang="ku" data-title="Proteîn" data-language-autonym="Kurdî" data-language-local-name="Kurdish" class="interlanguage-link-target"><span>Kurdî</span></a></li><li class="interlanguage-link interwiki-ky mw-list-item"><a href="https://ky.wikipedia.org/wiki/%D0%91%D0%B5%D0%BB%D0%BE%D0%BA" title="Белок – Kyrgyz" lang="ky" hreflang="ky" data-title="Белок" data-language-autonym="Кыргызча" data-language-local-name="Kyrgyz" class="interlanguage-link-target"><span>Кыргызча</span></a></li><li class="interlanguage-link interwiki-lo mw-list-item"><a href="https://lo.wikipedia.org/wiki/%E0%BA%9B%E0%BA%B0%E0%BB%82%E0%BA%A5%E0%BB%80%E0%BA%95%E0%BA%AD%E0%BA%B4%E0%BA%99" title="ປະໂລເຕອິນ – Lao" lang="lo" hreflang="lo" data-title="ປະໂລເຕອິນ" data-language-autonym="ລາວ" data-language-local-name="Lao" class="interlanguage-link-target"><span>ລາວ</span></a></li><li class="interlanguage-link interwiki-la mw-list-item"><a href="https://la.wikipedia.org/wiki/Proteina" title="Proteina – Latin" lang="la" hreflang="la" data-title="Proteina" data-language-autonym="Latina" data-language-local-name="Latin" class="interlanguage-link-target"><span>Latina</span></a></li><li class="interlanguage-link interwiki-lv mw-list-item"><a href="https://lv.wikipedia.org/wiki/Olbaltumvielas" title="Olbaltumvielas – Latvian" lang="lv" hreflang="lv" data-title="Olbaltumvielas" data-language-autonym="Latviešu" data-language-local-name="Latvian" class="interlanguage-link-target"><span>Latviešu</span></a></li><li class="interlanguage-link interwiki-lb mw-list-item"><a href="https://lb.wikipedia.org/wiki/Protein" title="Protein – Luxembourgish" lang="lb" hreflang="lb" data-title="Protein" data-language-autonym="Lëtzebuergesch" data-language-local-name="Luxembourgish" class="interlanguage-link-target"><span>Lëtzebuergesch</span></a></li><li class="interlanguage-link interwiki-lez mw-list-item"><a href="https://lez.wikipedia.org/wiki/%D0%9B%D0%B0%D0%B4%D0%B7%D0%B0%D1%80" title="Ладзар – Lezghian" lang="lez" hreflang="lez" data-title="Ладзар" data-language-autonym="Лезги" data-language-local-name="Lezghian" class="interlanguage-link-target"><span>Лезги</span></a></li><li class="interlanguage-link interwiki-lt mw-list-item"><a href="https://lt.wikipedia.org/wiki/Baltymai" title="Baltymai – Lithuanian" lang="lt" hreflang="lt" data-title="Baltymai" data-language-autonym="Lietuvių" data-language-local-name="Lithuanian" class="interlanguage-link-target"><span>Lietuvių</span></a></li><li class="interlanguage-link interwiki-li mw-list-item"><a href="https://li.wikipedia.org/wiki/Prote%C3%AFne" title="Proteïne – Limburgish" lang="li" hreflang="li" data-title="Proteïne" data-language-autonym="Limburgs" data-language-local-name="Limburgish" class="interlanguage-link-target"><span>Limburgs</span></a></li><li class="interlanguage-link interwiki-lfn mw-list-item"><a href="https://lfn.wikipedia.org/wiki/Protena" title="Protena – Lingua Franca Nova" lang="lfn" hreflang="lfn" data-title="Protena" data-language-autonym="Lingua Franca Nova" data-language-local-name="Lingua Franca Nova" class="interlanguage-link-target"><span>Lingua Franca Nova</span></a></li><li class="interlanguage-link interwiki-lmo mw-list-item"><a href="https://lmo.wikipedia.org/wiki/Pruteina" title="Pruteina – Lombard" lang="lmo" hreflang="lmo" data-title="Pruteina" data-language-autonym="Lombard" data-language-local-name="Lombard" class="interlanguage-link-target"><span>Lombard</span></a></li><li class="interlanguage-link interwiki-hu mw-list-item"><a href="https://hu.wikipedia.org/wiki/Feh%C3%A9rje" title="Fehérje – Hungarian" lang="hu" hreflang="hu" data-title="Fehérje" data-language-autonym="Magyar" data-language-local-name="Hungarian" class="interlanguage-link-target"><span>Magyar</span></a></li><li class="interlanguage-link interwiki-mk mw-list-item"><a href="https://mk.wikipedia.org/wiki/%D0%91%D0%B5%D0%BB%D0%BA%D0%BE%D0%B2%D0%B8%D0%BD%D0%B0" title="Белковина – Macedonian" lang="mk" hreflang="mk" data-title="Белковина" data-language-autonym="Македонски" data-language-local-name="Macedonian" class="interlanguage-link-target"><span>Македонски</span></a></li><li class="interlanguage-link interwiki-mg mw-list-item"><a href="https://mg.wikipedia.org/wiki/Pr%C3%B4teinina" title="Prôteinina – Malagasy" lang="mg" hreflang="mg" data-title="Prôteinina" data-language-autonym="Malagasy" data-language-local-name="Malagasy" class="interlanguage-link-target"><span>Malagasy</span></a></li><li class="interlanguage-link interwiki-ml mw-list-item"><a href="https://ml.wikipedia.org/wiki/%E0%B4%AE%E0%B4%BE%E0%B4%82%E0%B4%B8%E0%B5%8D%E0%B4%AF%E0%B4%82" title="മാംസ്യം – Malayalam" lang="ml" hreflang="ml" data-title="മാംസ്യം" data-language-autonym="മലയാളം" data-language-local-name="Malayalam" class="interlanguage-link-target"><span>മലയാളം</span></a></li><li class="interlanguage-link interwiki-mr mw-list-item"><a href="https://mr.wikipedia.org/wiki/%E0%A4%AA%E0%A5%8D%E0%A4%B0%E0%A4%A5%E0%A4%BF%E0%A4%A8%E0%A5%87" title="प्रथिने – Marathi" lang="mr" hreflang="mr" data-title="प्रथिने" data-language-autonym="मराठी" data-language-local-name="Marathi" class="interlanguage-link-target"><span>मराठी</span></a></li><li class="interlanguage-link interwiki-xmf mw-list-item"><a href="https://xmf.wikipedia.org/wiki/%E1%83%AA%E1%83%98%E1%83%9A%E1%83%94%E1%83%A4%E1%83%98" title="ცილეფი – Mingrelian" lang="xmf" hreflang="xmf" data-title="ცილეფი" data-language-autonym="მარგალური" data-language-local-name="Mingrelian" class="interlanguage-link-target"><span>მარგალური</span></a></li><li class="interlanguage-link interwiki-arz mw-list-item"><a href="https://arz.wikipedia.org/wiki/%D8%A8%D8%B1%D9%88%D8%AA%D9%8A%D9%86" title="بروتين – Egyptian Arabic" lang="arz" hreflang="arz" data-title="بروتين" data-language-autonym="مصرى" data-language-local-name="Egyptian Arabic" class="interlanguage-link-target"><span>مصرى</span></a></li><li class="interlanguage-link interwiki-mzn mw-list-item"><a href="https://mzn.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D8%AA%DB%8C%D9%86" title="پروتین – Mazanderani" lang="mzn" hreflang="mzn" data-title="پروتین" data-language-autonym="مازِرونی" data-language-local-name="Mazanderani" class="interlanguage-link-target"><span>مازِرونی</span></a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Protein" title="Protein – Malay" lang="ms" hreflang="ms" data-title="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-cdo mw-list-item"><a href="https://cdo.wikipedia.org/wiki/L%C3%A2ung-b%C4%83h-c%C3%A9k" title="Lâung-băh-cék – Mindong" lang="cdo" hreflang="cdo" data-title="Lâung-băh-cék" data-language-autonym="閩東語 / Mìng-dĕ̤ng-ngṳ̄" data-language-local-name="Mindong" class="interlanguage-link-target"><span>閩東語 / Mìng-dĕ̤ng-ngṳ̄</span></a></li><li class="interlanguage-link interwiki-mn mw-list-item"><a href="https://mn.wikipedia.org/wiki/%D0%A3%D1%83%D1%80%D0%B0%D0%B3_(%D0%BC%D0%BE%D0%BB%D0%B5%D0%BA%D1%83%D0%BB)" title="Уураг (молекул) – Mongolian" lang="mn" hreflang="mn" data-title="Уураг (молекул)" data-language-autonym="Монгол" data-language-local-name="Mongolian" class="interlanguage-link-target"><span>Монгол</span></a></li><li class="interlanguage-link interwiki-my mw-list-item"><a href="https://my.wikipedia.org/wiki/%E1%80%95%E1%80%9B%E1%80%AD%E1%80%AF%E1%80%90%E1%80%AD%E1%80%94%E1%80%BA%E1%80%B8" title="ပရိုတိန်း – Burmese" lang="my" hreflang="my" data-title="ပရိုတိန်း" data-language-autonym="မြန်မာဘာသာ" data-language-local-name="Burmese" class="interlanguage-link-target"><span>မြန်မာဘာသာ</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Eiwitten" title="Eiwitten – Dutch" lang="nl" hreflang="nl" data-title="Eiwitten" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-ne mw-list-item"><a href="https://ne.wikipedia.org/wiki/%E0%A4%AA%E0%A5%8D%E0%A4%B0%E0%A5%8B%E0%A4%9F%E0%A4%BF%E0%A4%A8" title="प्रोटिन – Nepali" lang="ne" hreflang="ne" data-title="प्रोटिन" data-language-autonym="नेपाली" data-language-local-name="Nepali" class="interlanguage-link-target"><span>नेपाली</span></a></li><li class="interlanguage-link interwiki-new mw-list-item"><a href="https://new.wikipedia.org/wiki/%E0%A4%AA%E0%A5%8D%E0%A4%B0%E0%A5%8B%E0%A4%9F%E0%A4%BF%E0%A4%A8" title="प्रोटिन – Newari" lang="new" hreflang="new" data-title="प्रोटिन" data-language-autonym="नेपाल भाषा" data-language-local-name="Newari" class="interlanguage-link-target"><span>नेपाल भाषा</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%BF%E3%83%B3%E3%83%91%E3%82%AF%E8%B3%AA" title="タンパク質 – Japanese" lang="ja" hreflang="ja" data-title="タンパク質" 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-ce mw-list-item"><a href="https://ce.wikipedia.org/wiki/%D0%91%D0%B5%D0%BB%D0%BE%D0%BA%D0%B0%D1%88" title="Белокаш – Chechen" lang="ce" hreflang="ce" data-title="Белокаш" data-language-autonym="Нохчийн" data-language-local-name="Chechen" class="interlanguage-link-target"><span>Нохчийн</span></a></li><li class="interlanguage-link interwiki-frr mw-list-item"><a href="https://frr.wikipedia.org/wiki/Proteiin" title="Proteiin – Northern Frisian" lang="frr" hreflang="frr" data-title="Proteiin" data-language-autonym="Nordfriisk" data-language-local-name="Northern Frisian" class="interlanguage-link-target"><span>Nordfriisk</span></a></li><li class="interlanguage-link interwiki-no mw-list-item"><a href="https://no.wikipedia.org/wiki/Protein" title="Protein – Norwegian Bokmål" lang="nb" hreflang="nb" data-title="Protein" data-language-autonym="Norsk bokmål" data-language-local-name="Norwegian Bokmål" class="interlanguage-link-target"><span>Norsk bokmål</span></a></li><li class="interlanguage-link interwiki-nn mw-list-item"><a href="https://nn.wikipedia.org/wiki/Protein" title="Protein – Norwegian Nynorsk" lang="nn" hreflang="nn" data-title="Protein" data-language-autonym="Norsk nynorsk" data-language-local-name="Norwegian Nynorsk" class="interlanguage-link-target"><span>Norsk nynorsk</span></a></li><li class="interlanguage-link interwiki-nov mw-list-item"><a href="https://nov.wikipedia.org/wiki/Proteine" title="Proteine – Novial" lang="nov" hreflang="nov" data-title="Proteine" data-language-autonym="Novial" data-language-local-name="Novial" class="interlanguage-link-target"><span>Novial</span></a></li><li class="interlanguage-link interwiki-oc mw-list-item"><a href="https://oc.wikipedia.org/wiki/Prote%C3%AFna" title="Proteïna – Occitan" lang="oc" hreflang="oc" data-title="Proteïna" data-language-autonym="Occitan" data-language-local-name="Occitan" class="interlanguage-link-target"><span>Occitan</span></a></li><li class="interlanguage-link interwiki-or mw-list-item"><a href="https://or.wikipedia.org/wiki/%E0%AC%AA%E0%AD%81%E0%AC%B7%E0%AD%8D%E0%AC%9F%E0%AC%BF%E0%AC%B8%E0%AC%BE%E0%AC%B0" title="ପୁଷ୍ଟିସାର – Odia" lang="or" hreflang="or" data-title="ପୁଷ୍ଟିସାର" data-language-autonym="ଓଡ଼ିଆ" data-language-local-name="Odia" class="interlanguage-link-target"><span>ଓଡ଼ିଆ</span></a></li><li class="interlanguage-link interwiki-om mw-list-item"><a href="https://om.wikipedia.org/wiki/Burqata" title="Burqata – Oromo" lang="om" hreflang="om" data-title="Burqata" data-language-autonym="Oromoo" data-language-local-name="Oromo" class="interlanguage-link-target"><span>Oromoo</span></a></li><li class="interlanguage-link interwiki-uz mw-list-item"><a href="https://uz.wikipedia.org/wiki/Proteinlar" title="Proteinlar – Uzbek" lang="uz" hreflang="uz" data-title="Proteinlar" 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-pa mw-list-item"><a href="https://pa.wikipedia.org/wiki/%E0%A8%AA%E0%A9%8D%E0%A8%B0%E0%A9%8B%E0%A8%9F%E0%A9%80%E0%A8%A8" title="ਪ੍ਰੋਟੀਨ – Punjabi" lang="pa" hreflang="pa" data-title="ਪ੍ਰੋਟੀਨ" data-language-autonym="ਪੰਜਾਬੀ" data-language-local-name="Punjabi" class="interlanguage-link-target"><span>ਪੰਜਾਬੀ</span></a></li><li class="interlanguage-link interwiki-pnb mw-list-item"><a href="https://pnb.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D9%B9%DB%8C%D9%86" title="پروٹین – Western Punjabi" lang="pnb" hreflang="pnb" data-title="پروٹین" data-language-autonym="پنجابی" data-language-local-name="Western Punjabi" class="interlanguage-link-target"><span>پنجابی</span></a></li><li class="interlanguage-link interwiki-blk mw-list-item"><a href="https://blk.wikipedia.org/wiki/%E1%80%95%E1%80%9B%E1%80%AD%E1%80%AF%E1%80%90%E1%80%B1%E1%80%84%E1%80%BA%E1%80%B8" title="ပရိုတေင်း – Pa'O" lang="blk" hreflang="blk" data-title="ပရိုတေင်း" data-language-autonym="ပအိုဝ်ႏဘာႏသာႏ" data-language-local-name="Pa'O" class="interlanguage-link-target"><span>ပအိုဝ်ႏဘာႏသာႏ</span></a></li><li class="interlanguage-link interwiki-ps mw-list-item"><a href="https://ps.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D9%BC%D9%8A%D9%86" title="پروټين – Pashto" lang="ps" hreflang="ps" data-title="پروټين" data-language-autonym="پښتو" data-language-local-name="Pashto" class="interlanguage-link-target"><span>پښتو</span></a></li><li class="interlanguage-link interwiki-pms mw-list-item"><a href="https://pms.wikipedia.org/wiki/Protein-a" title="Protein-a – Piedmontese" lang="pms" hreflang="pms" data-title="Protein-a" data-language-autonym="Piemontèis" data-language-local-name="Piedmontese" class="interlanguage-link-target"><span>Piemontèis</span></a></li><li class="interlanguage-link interwiki-nds mw-list-item"><a href="https://nds.wikipedia.org/wiki/Protein" title="Protein – Low German" lang="nds" hreflang="nds" data-title="Protein" data-language-autonym="Plattdüütsch" data-language-local-name="Low German" class="interlanguage-link-target"><span>Plattdüütsch</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Bia%C5%82ka" title="Białka – Polish" lang="pl" hreflang="pl" data-title="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 badge-Q17437796 badge-featuredarticle mw-list-item" title="featured article badge"><a href="https://pt.wikipedia.org/wiki/Prote%C3%ADna" title="Proteína – Portuguese" lang="pt" hreflang="pt" data-title="Proteína" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Protein%C4%83" title="Proteină – Romanian" lang="ro" hreflang="ro" data-title="Proteină" data-language-autonym="Română" data-language-local-name="Romanian" class="interlanguage-link-target"><span>Română</span></a></li><li class="interlanguage-link interwiki-qu mw-list-item"><a href="https://qu.wikipedia.org/wiki/Prutina" title="Prutina – Quechua" lang="qu" hreflang="qu" data-title="Prutina" data-language-autonym="Runa Simi" data-language-local-name="Quechua" class="interlanguage-link-target"><span>Runa Simi</span></a></li><li class="interlanguage-link interwiki-rue mw-list-item"><a href="https://rue.wikipedia.org/wiki/%D0%9F%D1%80%D0%BE%D1%82%D0%B5%D1%96%D0%BD" title="Протеін – Rusyn" lang="rue" hreflang="rue" data-title="Протеін" data-language-autonym="Русиньскый" data-language-local-name="Rusyn" class="interlanguage-link-target"><span>Русиньскый</span></a></li><li class="interlanguage-link interwiki-ru badge-Q17437796 badge-featuredarticle mw-list-item" title="featured article badge"><a href="https://ru.wikipedia.org/wiki/%D0%91%D0%B5%D0%BB%D0%BA%D0%B8" title="Белки – Russian" lang="ru" hreflang="ru" data-title="Белки" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sah mw-list-item"><a href="https://sah.wikipedia.org/wiki/%D0%9F%D1%80%D0%BE%D1%82%D0%B5%D0%B8%D0%BD" title="Протеин – Yakut" lang="sah" hreflang="sah" data-title="Протеин" data-language-autonym="Саха тыла" data-language-local-name="Yakut" class="interlanguage-link-target"><span>Саха тыла</span></a></li><li class="interlanguage-link interwiki-skr mw-list-item"><a href="https://skr.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D9%B9%DB%8C%D9%86" title="پروٹین – Saraiki" lang="skr" hreflang="skr" data-title="پروٹین" data-language-autonym="سرائیکی" data-language-local-name="Saraiki" class="interlanguage-link-target"><span>سرائیکی</span></a></li><li class="interlanguage-link interwiki-sco mw-list-item"><a href="https://sco.wikipedia.org/wiki/Protein" title="Protein – Scots" lang="sco" hreflang="sco" data-title="Protein" data-language-autonym="Scots" data-language-local-name="Scots" class="interlanguage-link-target"><span>Scots</span></a></li><li class="interlanguage-link interwiki-stq mw-list-item"><a href="https://stq.wikipedia.org/wiki/Oaiwiete" title="Oaiwiete – Saterland Frisian" lang="stq" hreflang="stq" data-title="Oaiwiete" data-language-autonym="Seeltersk" data-language-local-name="Saterland Frisian" class="interlanguage-link-target"><span>Seeltersk</span></a></li><li class="interlanguage-link interwiki-sq mw-list-item"><a href="https://sq.wikipedia.org/wiki/Proteina" title="Proteina – Albanian" lang="sq" hreflang="sq" data-title="Proteina" data-language-autonym="Shqip" data-language-local-name="Albanian" class="interlanguage-link-target"><span>Shqip</span></a></li><li class="interlanguage-link interwiki-scn mw-list-item"><a href="https://scn.wikipedia.org/wiki/Pruti%C3%ACna" title="Prutiìna – Sicilian" lang="scn" hreflang="scn" data-title="Prutiìna" data-language-autonym="Sicilianu" data-language-local-name="Sicilian" class="interlanguage-link-target"><span>Sicilianu</span></a></li><li class="interlanguage-link interwiki-si mw-list-item"><a href="https://si.wikipedia.org/wiki/%E0%B6%B4%E0%B7%8A%E2%80%8D%E0%B6%BB%E0%B7%9D%E0%B6%A7%E0%B7%93%E0%B6%B1%E0%B7%8A" title="ප්‍රෝටීන් – Sinhala" lang="si" hreflang="si" data-title="ප්‍රෝටීන්" data-language-autonym="සිංහල" data-language-local-name="Sinhala" class="interlanguage-link-target"><span>සිංහල</span></a></li><li class="interlanguage-link interwiki-simple mw-list-item"><a href="https://simple.wikipedia.org/wiki/Protein" title="Protein – Simple English" lang="en-simple" hreflang="en-simple" data-title="Protein" data-language-autonym="Simple English" data-language-local-name="Simple English" class="interlanguage-link-target"><span>Simple English</span></a></li><li class="interlanguage-link interwiki-sd mw-list-item"><a href="https://sd.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D9%BD%D9%8A%D9%86" title="پروٽين – Sindhi" lang="sd" hreflang="sd" data-title="پروٽين" data-language-autonym="سنڌي" data-language-local-name="Sindhi" class="interlanguage-link-target"><span>سنڌي</span></a></li><li class="interlanguage-link interwiki-sk mw-list-item"><a href="https://sk.wikipedia.org/wiki/Bielkovina" title="Bielkovina – Slovak" lang="sk" hreflang="sk" data-title="Bielkovina" data-language-autonym="Slovenčina" data-language-local-name="Slovak" class="interlanguage-link-target"><span>Slovenčina</span></a></li><li class="interlanguage-link interwiki-sl mw-list-item"><a href="https://sl.wikipedia.org/wiki/Beljakovina" title="Beljakovina – Slovenian" lang="sl" hreflang="sl" data-title="Beljakovina" data-language-autonym="Slovenščina" data-language-local-name="Slovenian" class="interlanguage-link-target"><span>Slovenščina</span></a></li><li class="interlanguage-link interwiki-so mw-list-item"><a href="https://so.wikipedia.org/wiki/Borotiin" title="Borotiin – Somali" lang="so" hreflang="so" data-title="Borotiin" data-language-autonym="Soomaaliga" data-language-local-name="Somali" class="interlanguage-link-target"><span>Soomaaliga</span></a></li><li class="interlanguage-link interwiki-ckb mw-list-item"><a href="https://ckb.wikipedia.org/wiki/%D9%BE%D8%B1%DB%86%D8%AA%DB%8C%D9%86" title="پرۆتین – Central Kurdish" lang="ckb" hreflang="ckb" data-title="پرۆتین" data-language-autonym="کوردی" data-language-local-name="Central Kurdish" class="interlanguage-link-target"><span>کوردی</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/%D0%9F%D1%80%D0%BE%D1%82%D0%B5%D0%B8%D0%BD" title="Протеин – Serbian" lang="sr" hreflang="sr" data-title="Протеин" 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/Protein" title="Protein – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Protein" 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-su mw-list-item"><a href="https://su.wikipedia.org/wiki/Prot%C3%A9in" title="Protéin – Sundanese" lang="su" hreflang="su" data-title="Protéin" data-language-autonym="Sunda" data-language-local-name="Sundanese" class="interlanguage-link-target"><span>Sunda</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Proteiini" title="Proteiini – Finnish" lang="fi" hreflang="fi" data-title="Proteiini" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Protein" title="Protein – Swedish" lang="sv" hreflang="sv" data-title="Protein" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-tl mw-list-item"><a href="https://tl.wikipedia.org/wiki/Protina" title="Protina – Tagalog" lang="tl" hreflang="tl" data-title="Protina" data-language-autonym="Tagalog" data-language-local-name="Tagalog" class="interlanguage-link-target"><span>Tagalog</span></a></li><li class="interlanguage-link interwiki-ta mw-list-item"><a href="https://ta.wikipedia.org/wiki/%E0%AE%AA%E0%AF%81%E0%AE%B0%E0%AE%A4%E0%AE%AE%E0%AF%8D" title="புரதம் – Tamil" lang="ta" hreflang="ta" data-title="புரதம்" data-language-autonym="தமிழ்" data-language-local-name="Tamil" class="interlanguage-link-target"><span>தமிழ்</span></a></li><li class="interlanguage-link interwiki-tt mw-list-item"><a href="https://tt.wikipedia.org/wiki/%D0%90%D0%BA%D1%81%D1%8B%D0%BC" title="Аксым – Tatar" lang="tt" hreflang="tt" data-title="Аксым" data-language-autonym="Татарча / tatarça" data-language-local-name="Tatar" class="interlanguage-link-target"><span>Татарча / tatarça</span></a></li><li class="interlanguage-link interwiki-te mw-list-item"><a href="https://te.wikipedia.org/wiki/%E0%B0%AE%E0%B0%BE%E0%B0%82%E0%B0%B8%E0%B0%95%E0%B1%83%E0%B0%A4%E0%B1%8D%E0%B0%A4%E0%B1%81%E0%B0%B2%E0%B1%81" title="మాంసకృత్తులు – Telugu" lang="te" hreflang="te" data-title="మాంసకృత్తులు" data-language-autonym="తెలుగు" data-language-local-name="Telugu" class="interlanguage-link-target"><span>తెలుగు</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B9%82%E0%B8%9B%E0%B8%A3%E0%B8%95%E0%B8%B5%E0%B8%99" title="โปรตีน – Thai" lang="th" hreflang="th" data-title="โปรตีน" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target"><span>ไทย</span></a></li><li class="interlanguage-link interwiki-tg mw-list-item"><a href="https://tg.wikipedia.org/wiki/%D0%A1%D0%B0%D1%84%D0%B5%D0%B4%D0%B0%D2%B3%D0%BE" title="Сафедаҳо – Tajik" lang="tg" hreflang="tg" data-title="Сафедаҳо" data-language-autonym="Тоҷикӣ" data-language-local-name="Tajik" class="interlanguage-link-target"><span>Тоҷикӣ</span></a></li><li class="interlanguage-link interwiki-chr mw-list-item"><a href="https://chr.wikipedia.org/wiki/%E1%8E%A0%E1%8F%93%E1%8E%B5%E1%8F%A5%E1%8F%8D%E1%8F%97%E1%8F%8D%E1%8E%A9" title="ᎠᏓᎵᏥᏍᏗᏍᎩ – Cherokee" lang="chr" hreflang="chr" data-title="ᎠᏓᎵᏥᏍᏗᏍᎩ" data-language-autonym="ᏣᎳᎩ" data-language-local-name="Cherokee" class="interlanguage-link-target"><span>ᏣᎳᎩ</span></a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Protein" title="Protein – Turkish" lang="tr" hreflang="tr" data-title="Protein" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target"><span>Türkçe</span></a></li><li class="interlanguage-link interwiki-tk mw-list-item"><a href="https://tk.wikipedia.org/wiki/Belok" title="Belok – Turkmen" lang="tk" hreflang="tk" data-title="Belok" data-language-autonym="Türkmençe" data-language-local-name="Turkmen" class="interlanguage-link-target"><span>Türkmençe</span></a></li><li class="interlanguage-link interwiki-tyv mw-list-item"><a href="https://tyv.wikipedia.org/wiki/%D0%91%D0%B5%D0%BB%D0%BE%D0%BA" title="Белок – Tuvinian" lang="tyv" hreflang="tyv" data-title="Белок" data-language-autonym="Тыва дыл" data-language-local-name="Tuvinian" class="interlanguage-link-target"><span>Тыва дыл</span></a></li><li class="interlanguage-link interwiki-uk badge-Q17437796 badge-featuredarticle mw-list-item" title="featured article badge"><a href="https://uk.wikipedia.org/wiki/%D0%91%D1%96%D0%BB%D0%BA%D0%B8" title="Білки – Ukrainian" lang="uk" hreflang="uk" data-title="Білки" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target"><span>Українська</span></a></li><li class="interlanguage-link interwiki-ur mw-list-item"><a href="https://ur.wikipedia.org/wiki/%D9%BE%D8%B1%D9%88%D9%B9%DB%8C%D9%86" title="پروٹین – Urdu" lang="ur" hreflang="ur" data-title="پروٹین" data-language-autonym="اردو" data-language-local-name="Urdu" class="interlanguage-link-target"><span>اردو</span></a></li><li class="interlanguage-link interwiki-vec mw-list-item"><a href="https://vec.wikipedia.org/wiki/Proteine" title="Proteine – Venetian" lang="vec" hreflang="vec" data-title="Proteine" data-language-autonym="Vèneto" data-language-local-name="Venetian" class="interlanguage-link-target"><span>Vèneto</span></a></li><li class="interlanguage-link interwiki-vi badge-Q17437798 badge-goodarticle mw-list-item" title="good article badge"><a href="https://vi.wikipedia.org/wiki/Protein" title="Protein – Vietnamese" lang="vi" hreflang="vi" data-title="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-wa mw-list-item"><a href="https://wa.wikipedia.org/wiki/Proteyene" title="Proteyene – Walloon" lang="wa" hreflang="wa" data-title="Proteyene" data-language-autonym="Walon" data-language-local-name="Walloon" class="interlanguage-link-target"><span>Walon</span></a></li><li class="interlanguage-link interwiki-zh-classical mw-list-item"><a href="https://zh-classical.wikipedia.org/wiki/%E6%9C%8A" title="朊 – Literary Chinese" lang="lzh" hreflang="lzh" data-title="朊" data-language-autonym="文言" data-language-local-name="Literary Chinese" class="interlanguage-link-target"><span>文言</span></a></li><li class="interlanguage-link interwiki-vls mw-list-item"><a href="https://vls.wikipedia.org/wiki/Prote%C3%AFne" title="Proteïne – West Flemish" lang="vls" hreflang="vls" data-title="Proteïne" data-language-autonym="West-Vlams" data-language-local-name="West Flemish" class="interlanguage-link-target"><span>West-Vlams</span></a></li><li class="interlanguage-link interwiki-war mw-list-item"><a href="https://war.wikipedia.org/wiki/Protina" title="Protina – Waray" lang="war" hreflang="war" data-title="Protina" data-language-autonym="Winaray" data-language-local-name="Waray" class="interlanguage-link-target"><span>Winaray</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" title="蛋白质 – Wu" lang="wuu" hreflang="wuu" data-title="蛋白质" data-language-autonym="吴语" data-language-local-name="Wu" class="interlanguage-link-target"><span>吴语</span></a></li><li class="interlanguage-link interwiki-yi mw-list-item"><a href="https://yi.wikipedia.org/wiki/%D7%A4%D7%A8%D7%90%D7%98%D7%A2%D7%90%D7%99%D7%9F" title="פראטעאין – Yiddish" lang="yi" hreflang="yi" data-title="פראטעאין" data-language-autonym="ייִדיש" data-language-local-name="Yiddish" class="interlanguage-link-target"><span>ייִדיש</span></a></li><li class="interlanguage-link interwiki-zh-yue mw-list-item"><a href="https://zh-yue.wikipedia.org/wiki/%E8%9B%8B%E7%99%BD%E8%B3%AA" title="蛋白質 – Cantonese" lang="yue" hreflang="yue" data-title="蛋白質" data-language-autonym="粵語" data-language-local-name="Cantonese" class="interlanguage-link-target"><span>粵語</span></a></li><li class="interlanguage-link interwiki-bat-smg mw-list-item"><a href="https://bat-smg.wikipedia.org/wiki/Balt%C4%ABms" title="Baltīms – Samogitian" lang="sgs" hreflang="sgs" data-title="Baltīms" data-language-autonym="Žemaitėška" data-language-local-name="Samogitian" class="interlanguage-link-target"><span>Žemaitėška</span></a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E8%9B%8B%E7%99%BD%E8%B4%A8" title="蛋白质 – Chinese" lang="zh" hreflang="zh" data-title="蛋白质" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target"><span>中文</span></a></li><li class="interlanguage-link interwiki-btm mw-list-item"><a href="https://btm.wikipedia.org/wiki/Protein" title="Protein – Batak Mandailing" lang="btm" hreflang="btm" data-title="Protein" data-language-autonym="Batak Mandailing" 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</div> </div> <div id="bodyContent" class="vector-body" aria-labelledby="firstHeading" data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> <div id="mw-indicator-good-star" class="mw-indicator"><div class="mw-parser-output"><span typeof="mw:File"><a href="/wiki/Wikipedia:Good_articles*" title="This is a good article. 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Click here for more information." src="//upload.wikimedia.org/wikipedia/en/thumb/9/94/Symbol_support_vote.svg/19px-Symbol_support_vote.svg.png" decoding="async" width="19" height="20" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/9/94/Symbol_support_vote.svg/29px-Symbol_support_vote.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/9/94/Symbol_support_vote.svg/39px-Symbol_support_vote.svg.png 2x" data-file-width="180" data-file-height="185" /></a></span></div></div> <div id="mw-indicator-pp-default" class="mw-indicator"><div class="mw-parser-output"><span typeof="mw:File"><a href="/wiki/Wikipedia:Protection_policy#semi" title="This article is semi-protected."><img alt="Page semi-protected" src="//upload.wikimedia.org/wikipedia/en/thumb/1/1b/Semi-protection-shackle.svg/20px-Semi-protection-shackle.svg.png" decoding="async" width="20" height="20" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/1/1b/Semi-protection-shackle.svg/30px-Semi-protection-shackle.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/1/1b/Semi-protection-shackle.svg/40px-Semi-protection-shackle.svg.png 2x" data-file-width="512" data-file-height="512" /></a></span></div></div> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></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">Biomolecule consisting of chains of amino acid residues</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 a class of molecules. For protein as a nutrient, see <a href="/wiki/Protein_(nutrient)" class="mw-redirect" title="Protein (nutrient)">Protein (nutrient)</a>. For other uses, see <a href="/wiki/Protein_(disambiguation)" class="mw-disambig" title="Protein (disambiguation)">Protein (disambiguation)</a>.</div> <p class="mw-empty-elt"> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Myoglobin.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/60/Myoglobin.png/220px-Myoglobin.png" decoding="async" width="220" height="223" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/60/Myoglobin.png/330px-Myoglobin.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/60/Myoglobin.png/440px-Myoglobin.png 2x" data-file-width="1159" data-file-height="1173" /></a><figcaption>A representation of the 3D structure of the protein <a href="/wiki/Myoglobin" title="Myoglobin">myoglobin</a> showing turquoise <a href="/wiki/Alpha_helix" title="Alpha helix">α-helices</a>. This protein was the first to have its structure solved by <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a>. Toward the right-center among the coils, a <a href="/wiki/Prosthetic_group" title="Prosthetic group">prosthetic group</a> called a <a href="/wiki/Heme_group" class="mw-redirect" title="Heme group">heme group</a> (shown in gray) with a bound oxygen molecule (red).</figcaption></figure> <p><b>Proteins</b> are large <a href="/wiki/Biomolecule" title="Biomolecule">biomolecules</a> and <a href="/wiki/Macromolecule" title="Macromolecule">macromolecules</a> that comprise one or more long chains of <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> <a href="/wiki/Residue_(biochemistry)" class="mw-redirect" title="Residue (biochemistry)">residues</a>. Proteins perform a vast array of functions within organisms, including <a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">catalysing metabolic reactions</a>, <a href="/wiki/DNA_replication" title="DNA replication">DNA replication</a>, <a href="/wiki/Cell_signaling" title="Cell signaling">responding to stimuli</a>, providing <a href="/wiki/Cytoskeleton" title="Cytoskeleton">structure to cells</a> and <a href="/wiki/Fibrous_protein" title="Fibrous protein">organisms</a>, and <a href="/wiki/Intracellular_transport" title="Intracellular transport">transporting molecules</a> from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the <a href="/wiki/Nucleic_acid_sequence" title="Nucleic acid sequence">nucleotide sequence</a> of their <a href="/wiki/Gene" title="Gene">genes</a>, and which usually results in <a href="/wiki/Protein_folding" title="Protein folding">protein folding</a> into a specific <a href="/wiki/Protein_structure" title="Protein structure">3D structure</a> that determines its activity. </p><p>A linear chain of amino acid residues is called a <a href="/wiki/Polypeptide" class="mw-redirect" title="Polypeptide">polypeptide</a>. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called <a href="/wiki/Peptide" title="Peptide">peptides</a>. The individual amino acid residues are bonded together by <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a> and adjacent amino acid residues. The <a href="/wiki/Protein_primary_structure" title="Protein primary structure">sequence</a> of amino acid residues in a protein is defined by the <a href="/wiki/DNA_sequencing" title="DNA sequencing">sequence</a> of a gene, which is encoded in the <a href="/wiki/Genetic_code" title="Genetic code">genetic code</a>. In general, the genetic code specifies 20 standard amino acids; but in certain organisms the genetic code can include <a href="/wiki/Selenocysteine" title="Selenocysteine">selenocysteine</a> and—in certain <a href="/wiki/Archaea" title="Archaea">archaea</a>—<a href="/wiki/Pyrrolysine" title="Pyrrolysine">pyrrolysine</a>. Shortly after or even during synthesis, the residues in a protein are often chemically modified by <a href="/wiki/Post-translational_modification" title="Post-translational modification">post-translational modification</a>, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Some proteins have non-peptide groups attached, which can be called <a href="/wiki/Prosthetic_group" title="Prosthetic group">prosthetic groups</a> or <a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">cofactors</a>. Proteins can work together to achieve a particular function, and they often associate to form stable <a href="/wiki/Protein_complex" title="Protein complex">protein complexes</a>. </p><p>Once formed, proteins only exist for a certain period and are then <a href="/wiki/Proteolysis#Protein_degradation" title="Proteolysis">degraded</a> and recycled by the cell's machinery through the process of <a href="/wiki/Protein_turnover" title="Protein turnover">protein turnover</a>. A protein's lifespan is measured in terms of its <a href="/wiki/Half-life" title="Half-life">half-life</a> and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable. </p><p>Like other biological macromolecules such as <a href="/wiki/Polysaccharide" title="Polysaccharide">polysaccharides</a> and <a href="/wiki/Nucleic_acid" title="Nucleic acid">nucleic acids</a>, proteins are essential parts of organisms and participate in virtually every process within <a href="/wiki/Cell_(biology)" title="Cell (biology)">cells</a>. Many proteins are <a href="/wiki/Enzyme" title="Enzyme">enzymes</a> that <a href="/wiki/Catalysis" title="Catalysis">catalyse</a> biochemical reactions and are vital to <a href="/wiki/Metabolism" title="Metabolism">metabolism</a>. Some proteins have structural or mechanical functions, such as <a href="/wiki/Actin" title="Actin">actin</a> and <a href="/wiki/Myosin" title="Myosin">myosin</a> in muscle, and the <a href="/wiki/Cytoskeleton" title="Cytoskeleton">cytoskeleton</a>'s scaffolding proteins that maintain cell shape. Other proteins are important in cell signaling, <a href="/wiki/Antibody" title="Antibody">immune responses</a>, <a href="/wiki/Cell_adhesion" title="Cell adhesion">cell adhesion</a>, and the <a href="/wiki/Cell_cycle" title="Cell cycle">cell cycle</a>. In animals, proteins are needed in the <a href="/wiki/Diet_(nutrition)" title="Diet (nutrition)">diet</a> to provide the <a href="/wiki/Essential_amino_acid" title="Essential amino acid">essential amino acids</a> that cannot be <a href="/wiki/Amino_acid_synthesis" title="Amino acid synthesis">synthesized</a>. <a href="/wiki/Digestion" title="Digestion">Digestion</a> breaks the proteins down for metabolic use. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="History_and_etymology">History and etymology</h2></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/History_of_molecular_biology" title="History of molecular biology">History of molecular biology</a></div> <div class="mw-heading mw-heading3"><h3 id="Discovery_and_early_studies">Discovery and early studies</h3></div> <p>Proteins have been studied and recognized since the 1700s by <a href="/wiki/Antoine_Fran%C3%A7ois,_comte_de_Fourcroy" class="mw-redirect" title="Antoine François, comte de Fourcroy">Antoine Fourcroy</a> and others,<sup id="cite_ref-Osborne-1909_1-0" class="reference"><a href="#cite_note-Osborne-1909-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Reynolds2003_2-0" class="reference"><a href="#cite_note-Reynolds2003-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> who often collectively called them "<a href="/wiki/Albumin" title="Albumin">albumins</a>", or "albuminous materials" (<i>Eiweisskörper</i>, in German).<sup id="cite_ref-Reynolds2003_2-1" class="reference"><a href="#cite_note-Reynolds2003-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Gluten" title="Gluten">Gluten</a>, for example, was first separated from wheat in published research around 1747, and later determined to exist in many plants.<sup id="cite_ref-Osborne-1909_1-1" class="reference"><a href="#cite_note-Osborne-1909-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> In 1789, Antoine Fourcroy recognized three distinct varieties of animal proteins: <a href="/wiki/Albumin" title="Albumin">albumin</a>, <a href="/wiki/Fibrin" title="Fibrin">fibrin</a>, and <a href="/wiki/Gelatin" title="Gelatin">gelatin</a>.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> Vegetable (plant) proteins studied in the late 1700s and early 1800s included <a href="/wiki/Gluten" title="Gluten">gluten</a>, <a href="/wiki/Albumin" title="Albumin">plant albumin</a>, <a href="/wiki/Gliadin" title="Gliadin">gliadin</a>, and <a href="/wiki/Legumin" title="Legumin">legumin</a>.<sup id="cite_ref-Osborne-1909_1-2" class="reference"><a href="#cite_note-Osborne-1909-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> </p><p>Proteins were first described by the Dutch chemist <a href="/wiki/Gerardus_Johannes_Mulder" title="Gerardus Johannes Mulder">Gerardus Johannes Mulder</a> and named by the Swedish chemist <a href="/wiki/J%C3%B6ns_Jacob_Berzelius" title="Jöns Jacob Berzelius">Jöns Jacob Berzelius</a> in 1838.<sup id="cite_ref-Mulder1938_4-0" class="reference"><a href="#cite_note-Mulder1938-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Hartley_5-0" class="reference"><a href="#cite_note-Hartley-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Mulder carried out <a href="/wiki/Elemental_analysis" title="Elemental analysis">elemental analysis</a> of common proteins and found that nearly all proteins had the same <a href="/wiki/Empirical_formula" title="Empirical formula">empirical formula</a>, C<sub>400</sub>H<sub>620</sub>N<sub>100</sub>O<sub>120</sub>P<sub>1</sub>S<sub>1</sub>.<sup id="cite_ref-Perrett2007_6-0" class="reference"><a href="#cite_note-Perrett2007-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> He came to the erroneous conclusion that they might be composed of a single type of (very large) molecule. The term "protein" to describe these molecules was proposed by Mulder's associate Berzelius; protein is derived from the <a href="/wiki/Greek_language" title="Greek language">Greek</a> word <span title="Greek-language text"><span lang="el" style="font-style: normal;">πρώτειος</span></span> (<span title="Greek-language romanization"><i lang="el-Latn">proteios</i></span>), meaning "primary",<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> "in the lead", or "standing in front",<sup id="cite_ref-Reynolds2003_2-2" class="reference"><a href="#cite_note-Reynolds2003-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> + <i><a href="https://en.wiktionary.org/wiki/-in#Suffix" class="extiw" title="wikt:-in">-in</a></i>. Mulder went on to identify the products of protein degradation such as the <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> <a href="/wiki/Leucine" title="Leucine">leucine</a> for which he found a (nearly correct) molecular weight of 131 <a href="/wiki/Atomic_mass_unit" class="mw-redirect" title="Atomic mass unit">Da</a>.<sup id="cite_ref-Perrett2007_6-1" class="reference"><a href="#cite_note-Perrett2007-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>Early nutritional scientists such as the German <a href="/wiki/Carl_von_Voit" title="Carl von Voit">Carl von Voit</a> believed that protein was the most important nutrient for maintaining the structure of the body, because it was generally believed that "flesh makes flesh."<sup id="cite_ref-Bischoff1860_8-0" class="reference"><a href="#cite_note-Bischoff1860-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> Around 1862, <a href="/wiki/Karl_Heinrich_Ritthausen" title="Karl Heinrich Ritthausen">Karl Heinrich Ritthausen</a> isolated the amino acid <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a>.<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> <a href="/wiki/Thomas_Burr_Osborne_(chemist)" title="Thomas Burr Osborne (chemist)">Thomas Burr Osborne</a> compiled a detailed review of the vegetable proteins at the <a href="/wiki/Connecticut_Agricultural_Experiment_Station" title="Connecticut Agricultural Experiment Station">Connecticut Agricultural Experiment Station</a>. Osborne, alongside <a href="/wiki/Lafayette_Mendel" title="Lafayette Mendel">Lafayette Mendel</a>, established several <a href="/wiki/Essential_amino_acid" title="Essential amino acid">nutritionally essential amino acids</a> in feeding experiments with laboratory rats.<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> Diets lacking an essential amino acid stunts the rats' growth, consistent with <a href="/wiki/Liebig%27s_law_of_the_minimum" title="Liebig's law of the minimum">Liebig's law of the minimum</a>.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> The final essential amino acid to be discovered, <a href="/wiki/Threonine" title="Threonine">threonine</a>, was identified by <a href="/wiki/William_Cumming_Rose" title="William Cumming Rose">William Cumming Rose</a>.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p><p>The difficulty in purifying proteins impeded work by early protein biochemists. Proteins could be obtained in large quantities from blood, egg whites, and <a href="/wiki/Keratin" title="Keratin">keratin</a>, but individual proteins were unavailable. In the 1950s, the <a href="/wiki/Armour_and_Company" title="Armour and Company">Armour Hot Dog Company</a> purified 1 kg of bovine pancreatic <a href="/wiki/Ribonuclease_A" class="mw-redirect" title="Ribonuclease A">ribonuclease A</a> and made it freely available to scientists. This gesture helped ribonuclease A become a major target for biochemical study for the following decades.<sup id="cite_ref-Perrett2007_6-2" class="reference"><a href="#cite_note-Perrett2007-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Polypeptides">Polypeptides</h3></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Peptide_bond.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/b/ba/Peptide_bond.jpg/220px-Peptide_bond.jpg" decoding="async" width="220" height="155" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/ba/Peptide_bond.jpg/330px-Peptide_bond.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/ba/Peptide_bond.jpg/440px-Peptide_bond.jpg 2x" data-file-width="873" data-file-height="614" /></a><figcaption>polypeptide</figcaption></figure> <p>The understanding of proteins as <a href="/wiki/Polypeptide" class="mw-redirect" title="Polypeptide">polypeptides</a>, or chains of amino acids, came through the work of <a href="/wiki/Franz_Hofmeister" title="Franz Hofmeister">Franz Hofmeister</a> and <a href="/wiki/Hermann_Emil_Fischer" class="mw-redirect" title="Hermann Emil Fischer">Hermann Emil Fischer</a> in 1902.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup><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> The central role of proteins as <a href="/wiki/Enzyme" title="Enzyme">enzymes</a> in living organisms that catalyzed reactions was not fully appreciated until 1926, when <a href="/wiki/James_B._Sumner" title="James B. Sumner">James B. Sumner</a> showed that the enzyme <a href="/wiki/Urease" title="Urease">urease</a> was in fact a protein.<sup id="cite_ref-Sumner1926_15-0" class="reference"><a href="#cite_note-Sumner1926-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Linus_Pauling" title="Linus Pauling">Linus Pauling</a> is credited with the successful prediction of regular protein <a href="/wiki/Secondary_structure" class="mw-redirect" title="Secondary structure">secondary structures</a> based on <a href="/wiki/Hydrogen_bonding" class="mw-redirect" title="Hydrogen bonding">hydrogen bonding</a>, an idea first put forth by <a href="/wiki/William_Astbury" title="William Astbury">William Astbury</a> in 1933.<sup id="cite_ref-Pauling1951_16-0" class="reference"><a href="#cite_note-Pauling1951-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> Later work by <a href="/wiki/Walter_Kauzmann" title="Walter Kauzmann">Walter Kauzmann</a> on <a href="/wiki/Denaturation_(biochemistry)" title="Denaturation (biochemistry)">denaturation</a>,<sup id="cite_ref-Kauzmann1956_17-0" class="reference"><a href="#cite_note-Kauzmann1956-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Kauzmann1959_18-0" class="reference"><a href="#cite_note-Kauzmann1959-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> based partly on previous studies by <a href="/wiki/Kaj_Ulrik_Linderstr%C3%B8m-Lang" title="Kaj Ulrik Linderstrøm-Lang">Kaj Linderstrøm-Lang</a>,<sup id="cite_ref-Kalman1955_19-0" class="reference"><a href="#cite_note-Kalman1955-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> contributed an understanding of <a href="/wiki/Protein_folding" title="Protein folding">protein folding</a> and structure mediated by <a href="/wiki/Hydrophobic_core" class="mw-redirect" title="Hydrophobic core">hydrophobic interactions</a>.<sup id="cite_ref-20" class="reference"><a href="#cite_note-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> </p><p>The first protein to have its amino acid chain <a href="/wiki/Protein_sequencing" title="Protein sequencing">sequenced</a> was <a href="/wiki/Insulin" title="Insulin">insulin</a>, by <a href="/wiki/Frederick_Sanger" title="Frederick Sanger">Frederick Sanger</a>, in 1949. Sanger correctly determined the amino acid sequence of insulin, thus conclusively demonstrating that proteins consisted of linear polymers of amino acids rather than branched chains, <a href="/wiki/Colloid" title="Colloid">colloids</a>, or <a href="/wiki/Cyclol" title="Cyclol">cyclols</a>.<sup id="cite_ref-Sanger1949_21-0" class="reference"><a href="#cite_note-Sanger1949-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> He won the Nobel Prize for this achievement in 1958.<sup id="cite_ref-Lecture_1958_22-0" class="reference"><a href="#cite_note-Lecture_1958-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Christian_Anfinsen" class="mw-redirect" title="Christian Anfinsen">Christian Anfinsen</a>'s studies of the <a href="/wiki/Oxidative_folding" title="Oxidative folding">oxidative folding</a> process of ribonuclease A, for which he won the nobel prize in 1972, solidified the <a href="/wiki/Thermodynamic_hypothesis" class="mw-redirect" title="Thermodynamic hypothesis">thermodynamic hypothesis</a> of protein folding, according to which the folded form of a protein represents its <a href="/wiki/Free_energy_(thermodynamics)" class="mw-redirect" title="Free energy (thermodynamics)">free energy</a> minimum.<sup id="cite_ref-pmid17754377_23-0" class="reference"><a href="#cite_note-pmid17754377-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-marshall_24-0" class="reference"><a href="#cite_note-marshall-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Structure">Structure</h3></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:KendrewMyoglobin.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/ec/KendrewMyoglobin.jpg/250px-KendrewMyoglobin.jpg" decoding="async" width="250" height="167" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/e/ec/KendrewMyoglobin.jpg 1.5x" data-file-width="340" data-file-height="227" /></a><figcaption><a href="/wiki/John_Kendrew" title="John Kendrew">John Kendrew</a> with model of myoglobin in progress</figcaption></figure> <p>With the development of <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a>, it became possible to determine protein structures as well as their sequences.<sup id="cite_ref-Stoddart_25-0" class="reference"><a href="#cite_note-Stoddart-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> The first <a href="/wiki/Protein_structure" title="Protein structure">protein structures</a> to be solved were <a href="/wiki/Hemoglobin" title="Hemoglobin">hemoglobin</a> by <a href="/wiki/Max_Perutz" title="Max Perutz">Max Perutz</a> and <a href="/wiki/Myoglobin" title="Myoglobin">myoglobin</a> by <a href="/wiki/John_Kendrew" title="John Kendrew">John Kendrew</a>, in 1958.<sup id="cite_ref-Muirhead1963_26-0" class="reference"><a href="#cite_note-Muirhead1963-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Kendrew1958_27-0" class="reference"><a href="#cite_note-Kendrew1958-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> The use of computers and increasing computing power has supported the sequencing of complex proteins. In 1999, <a href="/wiki/Roger_Kornberg" class="mw-redirect" title="Roger Kornberg">Roger Kornberg</a> sequenced the highly complex structure of <a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a> using high intensity X-rays from <a href="/wiki/Synchrotrons" class="mw-redirect" title="Synchrotrons">synchrotrons</a>.<sup id="cite_ref-Stoddart_25-1" class="reference"><a href="#cite_note-Stoddart-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> </p><p>Since then, <a href="/wiki/Cryo-electron_microscopy" class="mw-redirect" title="Cryo-electron microscopy">cryo-electron microscopy</a> (cryo-EM) of large <a href="/wiki/Macromolecular_Assembly" class="mw-redirect" title="Macromolecular Assembly">macromolecular assemblies</a><sup id="cite_ref-Zhou2008_28-0" class="reference"><a href="#cite_note-Zhou2008-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> has been developed. Cryo-EM uses protein samples that are frozen rather than crystals, and <a href="/wiki/Electron_microscopy" class="mw-redirect" title="Electron microscopy">beams of electrons</a> rather than X-rays. It causes less damage to the sample, allowing scientists to obtain more information and analyze larger structures.<sup id="cite_ref-Stoddart_25-2" class="reference"><a href="#cite_note-Stoddart-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Computational <a href="/wiki/Protein_structure_prediction" title="Protein structure prediction">protein structure prediction</a> of small protein <a href="/wiki/Structural_domain" class="mw-redirect" title="Structural domain">structural domains</a><sup id="cite_ref-Keskin2008_29-0" class="reference"><a href="#cite_note-Keskin2008-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> has helped researchers to approach atomic-level resolution of protein structures. As of April 2024<sup class="plainlinks noexcerpt noprint asof-tag update" style="display:none;"><a class="external text" href="https://en.wikipedia.org/w/index.php?title=Protein&action=edit">[update]</a></sup>, the <a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">Protein Data Bank</a> contains 181,018 X-ray, 19,809 <a href="/wiki/Cryogenic_electron_microscopy" title="Cryogenic electron microscopy">EM</a> and 12,697 <a href="/wiki/Protein_nuclear_magnetic_resonance_spectroscopy" class="mw-redirect" title="Protein nuclear magnetic resonance spectroscopy">NMR</a> protein structures.<sup id="cite_ref-30" class="reference"><a href="#cite_note-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Classification">Classification</h2></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main articles: <a href="/wiki/Protein_family" title="Protein family">Protein family</a>, <a href="/wiki/Gene_Ontology" title="Gene Ontology">Gene Ontology</a>, and <a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">Enzyme Commission number</a></div> <p>Proteins are primarily classified by sequence and structure, although other classifications are commonly used. Especially for enzymes the EC number system provides a functional classification scheme.<sup id="cite_ref-McDonald_Tipton_2023_31-0" class="reference"><a href="#cite_note-McDonald_Tipton_2023-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> Similarly, <a href="/wiki/Gene_Ontology" title="Gene Ontology">gene ontology</a> classifies both genes and proteins by their biological and biochemical function, and by their intracellular location.<sup id="cite_ref-pmid17984083_32-0" class="reference"><a href="#cite_note-pmid17984083-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </p><p>Sequence similarity is used to classify proteins both in terms of evolutionary and functional similarity. This may use either whole proteins or <a href="/wiki/Protein_domain" title="Protein domain">protein domains</a>, especially in <a href="/wiki/Protein_domain#Multidomain_proteins" title="Protein domain">multi-domain proteins</a>. Protein domains allow protein classification by a combination of sequence, structure and function, and they can be combined in many ways. In an early study of 170,000 proteins, about two-thirds were assigned at least one domain, with larger proteins containing more domains (e.g. proteins larger than 600 <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> having an average of more than 5 domains).<sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Biochemistry">Biochemistry</h2></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Peptide-Figure-Revised.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/c9/Peptide-Figure-Revised.png/300px-Peptide-Figure-Revised.png" decoding="async" width="300" height="231" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/c9/Peptide-Figure-Revised.png/450px-Peptide-Figure-Revised.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/c9/Peptide-Figure-Revised.png/600px-Peptide-Figure-Revised.png 2x" data-file-width="979" data-file-height="753" /></a><figcaption>Chemical structure of the peptide bond (bottom) and the three-dimensional structure of a peptide bond between an <a href="/wiki/Alanine" title="Alanine">alanine</a> and an adjacent amino acid (top/inset). The bond itself is made of the <a href="/wiki/CHON" class="mw-redirect" title="CHON">CHON</a> elements.</figcaption></figure> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Peptide_group_resonance.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/1/17/Peptide_group_resonance.png/300px-Peptide_group_resonance.png" decoding="async" width="300" height="65" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/1/17/Peptide_group_resonance.png 1.5x" data-file-width="393" data-file-height="85" /></a><figcaption><a href="/wiki/Resonance_(chemistry)" title="Resonance (chemistry)">Resonance</a> structures of the <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bond</a> that links individual amino acids to form a protein <a href="/wiki/Polymer" title="Polymer">polymer</a></figcaption></figure> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main articles: <a href="/wiki/Biochemistry" title="Biochemistry">Biochemistry</a>, <a href="/wiki/Amino_acid" title="Amino acid">Amino acid</a>, and <a href="/wiki/Peptide_bond" title="Peptide bond">Peptide bond</a></div> <p>Most proteins consist of linear <a href="/wiki/Polymer" title="Polymer">polymers</a> built from series of up to 20 <a href="/wiki/Chirality_(chemistry)#In_biochemistry" title="Chirality (chemistry)"><small>L</small>-α-amino</a> acids. All <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">proteinogenic amino acids</a> have a common structure where an <a href="/wiki/Alpha_carbon" class="mw-redirect" title="Alpha carbon">α-carbon</a> is <a href="/wiki/Chemical_bond" title="Chemical bond">bonded</a> to an <a href="/wiki/Amino" class="mw-redirect" title="Amino">amino</a> group, a <a href="/wiki/Carboxyl" class="mw-redirect" title="Carboxyl">carboxyl</a> group, and a variable <a href="/wiki/Side_chain" title="Side chain">side chain</a>. Only <a href="/wiki/Proline" title="Proline">proline</a> differs from this basic structure as its side chain is cyclical, bonding to the amino group, limiting protein chain flexibility.<sup id="cite_ref-Nelson2005_34-0" class="reference"><a href="#cite_note-Nelson2005-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> The side chains of the <a href="/wiki/List_of_standard_amino_acids" class="mw-redirect" title="List of standard amino acids">standard amino acids</a> have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and chemical reactivity.<sup id="cite_ref-Gutteridge2005_35-0" class="reference"><a href="#cite_note-Gutteridge2005-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> </p><p>The amino acids in a polypeptide chain are linked by <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a> between amino and carboxyl group. An individual amino acid in a chain is called a <i>residue,</i> and the linked series of carbon, nitrogen, and oxygen atoms are known as the <i>main chain</i> or <i>protein backbone.</i><sup id="cite_ref-Murray_2006_36-0" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 19">: 19 </span></sup> The peptide bond has two <a href="/wiki/Resonance_(chemistry)" title="Resonance (chemistry)">resonance</a> forms that confer some <a href="/wiki/Double-bond" class="mw-redirect" title="Double-bond">double-bond</a> character to the backbone. The alpha carbons are roughly <a href="/wiki/Coplanar" class="mw-redirect" title="Coplanar">coplanar</a> with the nitrogen and the carbonyl (C=O) group. The other two <a href="/wiki/Dihedral_angle" title="Dihedral angle">dihedral angles</a> in the peptide bond determine the local shape assumed by the protein backbone. One conseqence of the N-C(O) double bond character is that proteins are somewhat rigid.<sup id="cite_ref-Murray_2006_36-1" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 31">: 31 </span></sup> A polypeptide chain ends with a free amino group, known as the <i><a href="/wiki/N-terminus" title="N-terminus">N-terminus</a></i> or <i>amino terminus,</i> and a free carboxyl group, known as the <i><a href="/wiki/C-terminus" title="C-terminus">C-terminus</a></i> or <i>carboxy terminus</i>.<sup id="cite_ref-Reusch2013MSU_37-0" class="reference"><a href="#cite_note-Reusch2013MSU-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup> By convention, peptide sequences are written N-terminus to C-terminus, correlating with the order in which proteins are <a href="/wiki/Translation_(biology)" title="Translation (biology)">synthesized by ribosomes</a>.<sup id="cite_ref-Reusch2013MSU_37-1" class="reference"><a href="#cite_note-Reusch2013MSU-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-38" class="reference"><a href="#cite_note-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> </p><p>The words <i>protein</i>, <i>polypeptide,</i> and <i><a href="/wiki/Peptide" title="Peptide">peptide</a></i> are a little ambiguous and can overlap in meaning. <i>Protein</i> is generally used to refer to the complete biological molecule in a stable <a href="/wiki/Tertiary_structure" class="mw-redirect" title="Tertiary structure">conformation</a>, whereas <i>peptide</i> is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well defined and usually lies near 20–30 residues.<sup id="cite_ref-Lodish2004_39-0" class="reference"><a href="#cite_note-Lodish2004-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> </p><p>Proteins can interact with many types of molecules and ions, including <a href="/wiki/Protein%E2%80%93protein_interaction" title="Protein–protein interaction">with other proteins</a>, <a href="/wiki/Protein%E2%80%93lipid_interaction" title="Protein–lipid interaction">with lipids</a>, <a href="/wiki/Protein%E2%80%93carbohydrate_interaction" title="Protein–carbohydrate interaction">with carbohydrates</a>, and <a href="/wiki/Protein%E2%80%93DNA_interaction" class="mw-redirect" title="Protein–DNA interaction">with DNA</a>.<sup id="cite_ref-40" class="reference"><a href="#cite_note-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Brandon_1999_41-0" class="reference"><a href="#cite_note-Brandon_1999-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Van_Holde_1996_42-0" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Abundance_in_cells">Abundance in cells</h3></div> <p>A typical <a href="/wiki/Bacteria" title="Bacteria">bacterial</a> cell, e.g. <i><a href="/wiki/Escherichia_coli" title="Escherichia coli">E. coli</a></i> and <i><a href="/wiki/Staphylococcus_aureus" title="Staphylococcus aureus">Staphylococcus aureus</a></i>, is estimated to contain about 2 million proteins. Smaller bacteria, such as <i><a href="/wiki/Mycoplasma" title="Mycoplasma">Mycoplasma</a></i> or <i><a href="/wiki/Spirochaete" title="Spirochaete">spirochetes</a></i> contain fewer molecules, on the order of 50,000 to 1 million. By contrast, <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotic</a> cells are larger and thus contain much more protein. For instance, <a href="/wiki/Saccharomyces_cerevisiae" title="Saccharomyces cerevisiae">yeast</a> cells have been estimated to contain about 50 million proteins and <a href="/wiki/Human" title="Human">human</a> cells on the order of 1 to 3 billion.<sup id="cite_ref-43" class="reference"><a href="#cite_note-43"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup> The concentration of individual protein copies ranges from a few molecules per cell up to 20 million.<sup id="cite_ref-pmid22068332_44-0" class="reference"><a href="#cite_note-pmid22068332-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup> Not all genes coding proteins are expressed in most cells and their number depends on, for example, cell type and external stimuli. For instance, of the 20,000 or so proteins encoded by the human genome, only 6,000 are detected in <a href="/wiki/Lymphoblastoid" class="mw-redirect" title="Lymphoblastoid">lymphoblastoid</a> cells.<sup id="cite_ref-45" class="reference"><a href="#cite_note-45"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup> The most abundant protein in nature is thought to be <a href="/wiki/RuBisCO" title="RuBisCO">RuBisCO</a>, an enzyme that catalyzes the incorporation of <a href="/wiki/Carbon_dioxide" title="Carbon dioxide">carbon dioxide</a> into organic matter in <a href="/wiki/Photosynthesis" title="Photosynthesis">photosynthesis</a>. Plants can consist of as much as 1% by weight of this enzyme,<sup id="cite_ref-46" class="reference"><a href="#cite_note-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Synthesis">Synthesis</h2></div> <div class="mw-heading mw-heading3"><h3 id="Biosynthesis">Biosynthesis</h3></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Ribosome_mRNA_translation_en.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/b/b1/Ribosome_mRNA_translation_en.svg/220px-Ribosome_mRNA_translation_en.svg.png" decoding="async" width="220" height="155" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/b1/Ribosome_mRNA_translation_en.svg/330px-Ribosome_mRNA_translation_en.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/b1/Ribosome_mRNA_translation_en.svg/440px-Ribosome_mRNA_translation_en.svg.png 2x" data-file-width="512" data-file-height="361" /></a><figcaption>A ribosome produces a protein using mRNA as template</figcaption></figure> <figure class="mw-default-size skin-invert-image" typeof="mw:File/Thumb"><a href="/wiki/File:Genetic_code.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/3/37/Genetic_code.svg/220px-Genetic_code.svg.png" decoding="async" width="220" height="83" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/37/Genetic_code.svg/330px-Genetic_code.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/37/Genetic_code.svg/440px-Genetic_code.svg.png 2x" data-file-width="580" data-file-height="220" /></a><figcaption>The <a href="/wiki/DNA" title="DNA">DNA</a> sequence of a gene <a href="/wiki/Genetic_code" title="Genetic code">encodes</a> the amino acid sequence of a protein</figcaption></figure> <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_biosynthesis" title="Protein biosynthesis">Protein biosynthesis</a></div> <p>Proteins are assembled from amino acids using information encoded in genes. Each protein has its own unique amino acid sequence that is specified by the <a href="/wiki/Nucleotide" title="Nucleotide">nucleotide</a> sequence of the gene encoding this protein. The <a href="/wiki/Genetic_code" title="Genetic code">genetic code</a> is a set of three-nucleotide sets called <a href="/wiki/Codon" class="mw-redirect" title="Codon">codons</a> and each three-nucleotide combination designates an amino acid, for example AUG (<a href="/wiki/Adenine" title="Adenine">adenine</a>–<a href="/wiki/Uracil" title="Uracil">uracil</a>–<a href="/wiki/Guanine" title="Guanine">guanine</a>) is the code for <a href="/wiki/Methionine" title="Methionine">methionine</a>. Because <a href="/wiki/DNA" title="DNA">DNA</a> contains four nucleotides, the total number of possible codons is 64; hence, there is some redundancy in the genetic code, with some amino acids specified by more than one codon.<sup id="cite_ref-Van_Holde_1996_42-1" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 1002–42">: 1002–42 </span></sup> Genes encoded in DNA are first <a href="/wiki/Transcription_(genetics)" class="mw-redirect" title="Transcription (genetics)">transcribed</a> into pre-<a href="/wiki/Messenger_RNA" title="Messenger RNA">messenger RNA</a> (mRNA) by proteins such as <a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a>. Most organisms then process the pre-mRNA (a <i>primary transcript</i>) using various forms of <a href="/wiki/Post-transcriptional_modification" title="Post-transcriptional modification">post-transcriptional modification</a> to form the mature mRNA, which is then used as a template for protein synthesis by the <a href="/wiki/Ribosome" title="Ribosome">ribosome</a>. In <a href="/wiki/Prokaryote" title="Prokaryote">prokaryotes</a> the mRNA may either be used as soon as it is produced, or be bound by a ribosome after having moved away from the <a href="/wiki/Nucleoid" title="Nucleoid">nucleoid</a>. In contrast, <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> make mRNA in the <a href="/wiki/Cell_nucleus" title="Cell nucleus">cell nucleus</a> and then <a href="/wiki/Protein_translocation" class="mw-redirect" title="Protein translocation">translocate</a> it across the <a href="/wiki/Nuclear_membrane" class="mw-redirect" title="Nuclear membrane">nuclear membrane</a> into the <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a>, where <a href="/wiki/Protein_biosynthesis" title="Protein biosynthesis">protein synthesis</a> then takes place. The rate of protein synthesis is higher in prokaryotes than eukaryotes and can reach up to 20 amino acids per second.<sup id="cite_ref-Pain2000_47-0" class="reference"><a href="#cite_note-Pain2000-47"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup> </p><p>The process of synthesizing a protein from an mRNA template is known as <a href="/wiki/Translation_(genetics)" class="mw-redirect" title="Translation (genetics)">translation</a>. The mRNA is loaded onto the ribosome and is read three nucleotides at a time by matching each codon to its <a href="/wiki/Base_pair" title="Base pair">base pairing</a> <a href="/wiki/Anticodon" class="mw-redirect" title="Anticodon">anticodon</a> located on a <a href="/wiki/Transfer_RNA" title="Transfer RNA">transfer RNA</a> molecule, which carries the amino acid corresponding to the codon it recognizes. The enzyme <a href="/wiki/Aminoacyl_tRNA_synthetase" title="Aminoacyl tRNA synthetase">aminoacyl tRNA synthetase</a> "charges" the tRNA molecules with the correct amino acids. The growing polypeptide is often termed the <i>nascent chain</i>. Proteins are always biosynthesized from <a href="/wiki/N-terminus" title="N-terminus">N-terminus</a> to <a href="/wiki/C-terminus" title="C-terminus">C-terminus</a>.<sup id="cite_ref-Van_Holde_1996_42-2" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 1002–42">: 1002–42 </span></sup> </p><p>The size of a synthesized protein can be measured by the number of amino acids it contains and by its total <a href="/wiki/Molecular_mass" title="Molecular mass">molecular mass</a>, which is normally reported in units of <i>daltons</i> (synonymous with <a href="/wiki/Atomic_mass_unit" class="mw-redirect" title="Atomic mass unit">atomic mass units</a>), or the derivative unit kilodalton (kDa). The average size of a protein increases from Archaea to Bacteria to Eukaryote (283, 311, 438 residues and 31, 34, 49 kDa respectively) due to a bigger number of <a href="/wiki/Protein_domain" title="Protein domain">protein domains</a> constituting proteins in higher organisms.<sup id="cite_ref-Kozlowski2016_48-0" class="reference"><a href="#cite_note-Kozlowski2016-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> For instance, <a href="/wiki/Yeast" title="Yeast">yeast</a> proteins are on average 466 amino acids long and 53 kDa in mass.<sup id="cite_ref-Lodish2004_39-1" class="reference"><a href="#cite_note-Lodish2004-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> The largest known proteins are the <a href="/wiki/Titin" title="Titin">titins</a>, a component of the <a href="/wiki/Muscle" title="Muscle">muscle</a> <a href="/wiki/Sarcomere" title="Sarcomere">sarcomere</a>, with a molecular mass of almost 3,000 kDa and a total length of almost 27,000 amino acids.<sup id="cite_ref-Fulton1991_49-0" class="reference"><a href="#cite_note-Fulton1991-49"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Chemical_synthesis">Chemical synthesis</h3></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/Peptide_synthesis" title="Peptide synthesis">Peptide synthesis</a></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Peptide_Synthesis.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/c2/Peptide_Synthesis.svg/220px-Peptide_Synthesis.svg.png" decoding="async" width="220" height="99" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/c2/Peptide_Synthesis.svg/330px-Peptide_Synthesis.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/c2/Peptide_Synthesis.svg/440px-Peptide_Synthesis.svg.png 2x" data-file-width="692" data-file-height="310" /></a><figcaption>Peptide Synthesis</figcaption></figure> <p>Short proteins can be synthesized chemically by a family of <a href="/wiki/Peptide_synthesis" title="Peptide synthesis">peptide synthesis</a> methods. These rely on <a href="/wiki/Organic_synthesis" title="Organic synthesis">organic synthesis</a> techniques such as <a href="/wiki/Chemical_ligation" title="Chemical ligation">chemical ligation</a> to produce peptides in high yield.<sup id="cite_ref-Bruckdorfer2004_50-0" class="reference"><a href="#cite_note-Bruckdorfer2004-50"><span class="cite-bracket">[</span>50<span class="cite-bracket">]</span></a></sup> Chemical synthesis allows for the introduction of non-natural amino acids into polypeptide chains, such as attachment of <a href="/wiki/Fluorescent" class="mw-redirect" title="Fluorescent">fluorescent</a> probes to amino acid side chains.<sup id="cite_ref-Schwarzer2005_51-0" class="reference"><a href="#cite_note-Schwarzer2005-51"><span class="cite-bracket">[</span>51<span class="cite-bracket">]</span></a></sup> These methods are useful in laboratory <a href="/wiki/Biochemistry" title="Biochemistry">biochemistry</a> and <a href="/wiki/Cell_biology" title="Cell biology">cell biology</a>, though generally not for commercial applications. Chemical synthesis is inefficient for polypeptides longer than about 300 amino acids, and the synthesized proteins may not readily assume their native <a href="/wiki/Tertiary_structure" class="mw-redirect" title="Tertiary structure">tertiary structure</a>. Most chemical synthesis methods proceed from C-terminus to N-terminus, opposite the biological reaction.<sup id="cite_ref-Kent2009_52-0" class="reference"><a href="#cite_note-Kent2009-52"><span class="cite-bracket">[</span>52<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Structure_2">Structure</h2></div> <figure class="mw-default-size mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Chaperonin_1AON.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6c/Chaperonin_1AON.png/300px-Chaperonin_1AON.png" decoding="async" width="300" height="130" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6c/Chaperonin_1AON.png/450px-Chaperonin_1AON.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/6c/Chaperonin_1AON.png/600px-Chaperonin_1AON.png 2x" data-file-width="1956" data-file-height="850" /></a><figcaption>The crystal structure of the <a href="/wiki/Chaperonin" title="Chaperonin">chaperonin</a>, a huge protein complex. A single protein subunit is highlighted. Chaperonins assist protein folding.</figcaption></figure> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Proteinviews-1tim.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6e/Proteinviews-1tim.png/300px-Proteinviews-1tim.png" decoding="async" width="300" height="120" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6e/Proteinviews-1tim.png/450px-Proteinviews-1tim.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/6e/Proteinviews-1tim.png/600px-Proteinviews-1tim.png 2x" data-file-width="750" data-file-height="300" /></a><figcaption>Three possible representations of the three-dimensional structure of the protein <a href="/wiki/Triose_phosphate_isomerase" class="mw-redirect" title="Triose phosphate isomerase">triose phosphate isomerase</a>. <b>Left</b>: All-atom representation colored by atom type. <b>Middle:</b> Simplified representation illustrating the backbone conformation, colored by secondary structure. <b>Right</b>: Solvent-accessible surface representation colored by residue type (acidic residues red, basic residues blue, polar residues green, nonpolar residues white).</figcaption></figure> <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_structure" title="Protein structure">Protein structure</a></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Protein_structure_prediction" title="Protein structure prediction">Protein structure prediction</a></div> <p>Most proteins <a href="/wiki/Protein_folding" title="Protein folding">fold</a> into unique 3D structures. The shape into which a protein naturally folds is known as its <a href="/wiki/Native_conformation" class="mw-redirect" title="Native conformation">native conformation</a>.<sup id="cite_ref-Murray_2006_36-2" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 36">: 36 </span></sup> Although many proteins can fold unassisted, simply through the chemical properties of their amino acids, others require the aid of molecular <a href="/wiki/Chaperone_(protein)" title="Chaperone (protein)">chaperones</a> to fold into their native states.<sup id="cite_ref-Murray_2006_36-3" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 37">: 37 </span></sup> Biochemists often refer to four distinct aspects of a protein's structure:<sup id="cite_ref-Murray_2006_36-4" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 30–34">: 30–34 </span></sup> </p> <ul><li><i><a href="/wiki/Primary_structure" class="mw-redirect" title="Primary structure">Primary structure</a></i>: the <a href="/wiki/Peptide_sequence" class="mw-redirect" title="Peptide sequence">amino acid sequence</a>. A protein is a <a href="/wiki/Polyamide" title="Polyamide">polyamide</a>.</li> <li><i><a href="/wiki/Secondary_structure" class="mw-redirect" title="Secondary structure">Secondary structure</a></i>: regularly repeating local structures stabilized by <a href="/wiki/Hydrogen_bond" title="Hydrogen bond">hydrogen bonds</a>. The most common examples are the <a href="/wiki/Alpha_helix" title="Alpha helix">α-helix</a>, <a href="/wiki/Beta_sheet" title="Beta sheet">β-sheet</a> and <a href="/wiki/Turn_(biochemistry)" title="Turn (biochemistry)">turns</a>. Because secondary structures are local, many regions of distinct secondary structure can be present in the same protein molecule.</li> <li><i><a href="/wiki/Tertiary_structure" class="mw-redirect" title="Tertiary structure">Tertiary structure</a></i>: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a <a href="/wiki/Hydrophobic_core" class="mw-redirect" title="Hydrophobic core">hydrophobic core</a>, but also through <a href="/wiki/Salt_bridge_(protein)" class="mw-redirect" title="Salt bridge (protein)">salt bridges</a>, hydrogen bonds, <a href="/wiki/Disulfide_bond" class="mw-redirect" title="Disulfide bond">disulfide bonds</a>, and even <a href="/wiki/Posttranslational_modification" class="mw-redirect" title="Posttranslational modification">post-translational modifications</a>. The term "tertiary structure" is often used as synonymous with the term <i>fold</i>. The tertiary structure is what controls the basic function of the protein.</li> <li><i><a href="/wiki/Quaternary_structure" class="mw-redirect" title="Quaternary structure">Quaternary structure</a></i>: the structure formed by several protein molecules (polypeptide chains), usually called <i><a href="/wiki/Protein_subunit" title="Protein subunit">protein subunits</a></i> in this context, which function as a single <a href="/wiki/Protein_complex" title="Protein complex">protein complex</a>.</li> <li><i><a href="/wiki/Protein_quinary_structure" title="Protein quinary structure">Quinary structure</a></i>: the signatures of protein surface that organize the crowded cellular interior. Quinary structure is dependent on transient, yet essential, macromolecular interactions that occur inside living cells.</li></ul> <p>Proteins are not entirely rigid molecules. In addition to these levels of structure, proteins may shift between several related structures while they perform their functions. In the context of these functional rearrangements, these tertiary or quaternary structures are usually referred to as "<a href="/wiki/Chemical_conformation" class="mw-redirect" title="Chemical conformation">conformations</a>", and transitions between them are called <i>conformational changes.</i> Such changes are often induced by the binding of a <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> molecule to an enzyme's <a href="/wiki/Active_site" title="Active site">active site</a>, or the physical region of the protein that participates in chemical catalysis. In solution, protein structures vary because of thermal vibration and collisions with other molecules.<sup id="cite_ref-Van_Holde_1996_42-3" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 368–75">: 368–75 </span></sup> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Protein_composite.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/5/54/Protein_composite.png/300px-Protein_composite.png" decoding="async" width="300" height="78" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/5/54/Protein_composite.png/450px-Protein_composite.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/5/54/Protein_composite.png/600px-Protein_composite.png 2x" data-file-width="1600" data-file-height="416" /></a><figcaption>Molecular surface of several proteins showing their comparative sizes. From left to right are: <a href="/wiki/Immunoglobulin_G" title="Immunoglobulin G">immunoglobulin G</a> (IgG, an <a href="/wiki/Antibody" title="Antibody">antibody</a>), <a href="/wiki/Hemoglobin" title="Hemoglobin">hemoglobin</a>, <a href="/wiki/Insulin" title="Insulin">insulin</a> (a hormone), <a href="/wiki/Adenylate_kinase" title="Adenylate kinase">adenylate kinase</a> (an enzyme), and <a href="/wiki/Glutamine_synthetase" title="Glutamine synthetase">glutamine synthetase</a> (an enzyme).</figcaption></figure> <p>Proteins can be informally divided into three main classes, which correlate with typical tertiary structures: <a href="/wiki/Globular_protein" title="Globular protein">globular proteins</a>, <a href="/wiki/Fibrous_protein" title="Fibrous protein">fibrous proteins</a>, and <a href="/wiki/Membrane_protein" title="Membrane protein">membrane proteins</a>. Almost all globular proteins are <a href="/wiki/Soluble" class="mw-redirect" title="Soluble">soluble</a> and many are enzymes. Fibrous proteins are often structural, such as <a href="/wiki/Collagen" title="Collagen">collagen</a>, the major component of connective tissue, or <a href="/wiki/Keratin" title="Keratin">keratin</a>, the protein component of hair and nails. Membrane proteins often serve as <a href="/wiki/Receptor_(biochemistry)" title="Receptor (biochemistry)">receptors</a> or provide channels for polar or charged molecules to pass through the <a href="/wiki/Cell_membrane" title="Cell membrane">cell membrane</a>.<sup id="cite_ref-Van_Holde_1996_42-4" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 165–85">: 165–85 </span></sup> </p><p>A special case of intramolecular hydrogen bonds within proteins, poorly shielded from water attack and hence promoting their own <a href="/wiki/Dehydration" title="Dehydration">dehydration</a>, are called <a href="/wiki/Dehydron" class="mw-redirect" title="Dehydron">dehydrons</a>.<sup id="cite_ref-Fernandez2003_53-0" class="reference"><a href="#cite_note-Fernandez2003-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Protein_domains">Protein domains</h3></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_domain" title="Protein domain">Protein domain</a></div> <p>Many proteins are composed of several <a href="/wiki/Protein_domain" title="Protein domain">protein domains</a>, i.e. segments of a protein that fold into distinct structural units.<sup id="cite_ref-Biochemistry2010_54-0" class="reference"><a href="#cite_note-Biochemistry2010-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 134">: 134 </span></sup> Domains usually have specific functions, such as <a href="/wiki/Enzyme" title="Enzyme">enzymatic</a> activities (e.g. <a href="/wiki/Kinase" title="Kinase">kinase</a>) or they serve as binding modules.<sup id="cite_ref-Biochemistry2010_54-1" class="reference"><a href="#cite_note-Biochemistry2010-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 155–156">: 155–156 </span></sup> </p> <figure class="mw-halign-center" typeof="mw:File/Frame"><a href="/wiki/File:Domain_organisation_of_EVH_proteins.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/d/d8/Domain_organisation_of_EVH_proteins.png" decoding="async" width="691" height="187" class="mw-file-element" data-file-width="691" data-file-height="187" /></a><figcaption><b>Protein domains vs. motifs</b>. Protein domains (such as the <a href="/wiki/WH1_domain" title="WH1 domain">EVH1 domain</a>) are functional units within proteins that fold into defined 3D structures. Motifs are usually short sequences with specific functions but without a stable 3D structure. Many motifs are binding sites for other proteins (such as the red and green bars shown here in the context of a <a href="/wiki/Ena/Vasp_homology_proteins" title="Ena/Vasp homology proteins">VASP</a> protein).<sup id="cite_ref-55" class="reference"><a href="#cite_note-55"><span class="cite-bracket">[</span>55<span class="cite-bracket">]</span></a></sup></figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Sequence_motif">Sequence motif</h3></div> <p>Short amino acid sequences within proteins often act as recognition sites for other proteins.<sup id="cite_ref-56" class="reference"><a href="#cite_note-56"><span class="cite-bracket">[</span>56<span class="cite-bracket">]</span></a></sup> For instance, <a href="/wiki/SH3_domain" title="SH3 domain">SH3 domains</a> typically bind to short PxxP motifs (i.e. 2 <a href="/wiki/Proline" title="Proline">prolines</a> [P], separated by two unspecified <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> [x], although the surrounding amino acids may determine the exact binding specificity). Many such motifs has been collected in the <a href="/wiki/Eukaryotic_Linear_Motif_resource" title="Eukaryotic Linear Motif resource">Eukaryotic Linear Motif</a> (ELM) database.<sup id="cite_ref-57" class="reference"><a href="#cite_note-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Cellular_functions">Cellular functions</h2></div> <p>Proteins are the chief actors within the cell, said to be carrying out the duties specified by the information encoded in genes.<sup id="cite_ref-Lodish2004_39-2" class="reference"><a href="#cite_note-Lodish2004-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> With the exception of certain types of <a href="/wiki/RNA" title="RNA">RNA</a>, most other biological molecules are relatively inert elements upon which proteins act. Proteins make up half the dry weight of an <i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i> cell, whereas other macromolecules such as DNA and RNA make up only 3% and 20%, respectively.<sup id="cite_ref-Voet_58-0" class="reference"><a href="#cite_note-Voet-58"><span class="cite-bracket">[</span>58<span class="cite-bracket">]</span></a></sup> The set of proteins expressed in a particular cell or cell type is known as its <a href="/wiki/Proteome" title="Proteome">proteome</a>.<sup id="cite_ref-Biochemistry2010_54-2" class="reference"><a href="#cite_note-Biochemistry2010-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 120">: 120 </span></sup> </p> <figure class="mw-default-size mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Hexokinase_ball_and_stick_model,_with_substrates_to_scale_copy.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Hexokinase_ball_and_stick_model%2C_with_substrates_to_scale_copy.png/220px-Hexokinase_ball_and_stick_model%2C_with_substrates_to_scale_copy.png" decoding="async" width="220" height="145" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Hexokinase_ball_and_stick_model%2C_with_substrates_to_scale_copy.png/330px-Hexokinase_ball_and_stick_model%2C_with_substrates_to_scale_copy.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Hexokinase_ball_and_stick_model%2C_with_substrates_to_scale_copy.png/440px-Hexokinase_ball_and_stick_model%2C_with_substrates_to_scale_copy.png 2x" data-file-width="1760" data-file-height="1160" /></a><figcaption>The enzyme <a href="/wiki/Hexokinase" title="Hexokinase">hexokinase</a> is shown as a conventional ball-and-stick molecular model. To scale in the top right-hand corner are two of its substrates, <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a> and <a href="/wiki/Glucose" title="Glucose">glucose</a>.</figcaption></figure> <p>The chief characteristic of proteins that allows their diverse set of functions is their ability to bind other molecules specifically and tightly. The region of the protein responsible for binding another molecule is known as the <a href="/wiki/Binding_site" title="Binding site">binding site</a> and is often a depression or "pocket" on the molecular surface. This binding ability is mediated by the tertiary structure of the protein, which defines the binding site pocket, and by the chemical properties of the surrounding amino acids' side chains. Protein binding can be extraordinarily tight and specific; for example, the <a href="/wiki/Ribonuclease_inhibitor" title="Ribonuclease inhibitor">ribonuclease inhibitor</a> protein binds to human <a href="/wiki/Angiogenin" title="Angiogenin">angiogenin</a> with a sub-femtomolar <a href="/wiki/Dissociation_constant" title="Dissociation constant">dissociation constant</a> (<10<sup>−15</sup> M) but does not bind at all to its amphibian homolog <a href="/wiki/Onconase" class="mw-redirect" title="Onconase">onconase</a> (> 1 M). Extremely minor chemical changes such as the addition of a single methyl group to a binding partner can sometimes suffice to nearly eliminate binding; for example, the <a href="/wiki/Aminoacyl_tRNA_synthetase" title="Aminoacyl tRNA synthetase">aminoacyl tRNA synthetase</a> specific to the amino acid <a href="/wiki/Valine" title="Valine">valine</a> discriminates against the very similar side chain of the amino acid <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>.<sup id="cite_ref-Sankaranarayanan2001_59-0" class="reference"><a href="#cite_note-Sankaranarayanan2001-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup> </p><p>Proteins can bind to other proteins as well as to <a href="/wiki/Small_molecule" title="Small molecule">small-molecule</a> substrates. When proteins bind specifically to other copies of the same molecule, they can <a href="/wiki/Oligomer" title="Oligomer">oligomerize</a> to form fibrils; this process occurs often in structural proteins that consist of globular monomers that self-associate to form rigid fibers. <a href="/wiki/Protein%E2%80%93protein_interaction" title="Protein–protein interaction">Protein–protein interactions</a> regulate enzymatic activity, control progression through the <a href="/wiki/Cell_cycle" title="Cell cycle">cell cycle</a>, and allow the assembly of large <a href="/wiki/Protein_complex" title="Protein complex">protein complexes</a> that carry out many closely related reactions with a common biological function. Proteins can bind to, or be integrated into, cell membranes. The ability of binding partners to induce conformational changes in proteins allows the construction of enormously complex <a href="/wiki/Cell_signaling" title="Cell signaling">signaling</a> networks.<sup id="cite_ref-Van_Holde_1996_42-5" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 830–49">: 830–49 </span></sup> As interactions between proteins are reversible and depend heavily on the availability of different groups of partner proteins to form aggregates that are capable to carry out discrete sets of function, study of the interactions between specific proteins is a key to understand important aspects of cellular function, and ultimately the properties that distinguish particular cell types.<sup id="cite_ref-Copland2009_60-0" class="reference"><a href="#cite_note-Copland2009-60"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Samarin2009_61-0" class="reference"><a href="#cite_note-Samarin2009-61"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Enzymes">Enzymes</h3></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/Enzyme" title="Enzyme">Enzyme</a></div> <p>The best-known role of proteins in the cell is as <a href="/wiki/Enzyme" title="Enzyme">enzymes</a>, which <a href="/wiki/Catalysis" title="Catalysis">catalyse</a> chemical reactions. Enzymes are usually highly specific and accelerate only one or a few chemical reactions. Enzymes carry out most of the reactions involved in <a href="/wiki/Metabolism" title="Metabolism">metabolism</a>, as well as manipulating DNA in processes such as <a href="/wiki/DNA_replication" title="DNA replication">DNA replication</a>, <a href="/wiki/DNA_repair" title="DNA repair">DNA repair</a>, and <a href="/wiki/Transcription_(genetics)" class="mw-redirect" title="Transcription (genetics)">transcription</a>. Some enzymes act on other proteins to add or remove chemical groups in a process known as posttranslational modification. About 4,000 reactions are known to be catalysed by enzymes.<sup id="cite_ref-EXPASY2000_62-0" class="reference"><a href="#cite_note-EXPASY2000-62"><span class="cite-bracket">[</span>62<span class="cite-bracket">]</span></a></sup> The rate acceleration conferred by enzymatic catalysis is often enormous—as much as 10<sup>17</sup>-fold increase in rate over the uncatalysed reaction in the case of <a href="/wiki/Orotate_decarboxylase" class="mw-redirect" title="Orotate decarboxylase">orotate decarboxylase</a> (78 million years without the enzyme, 18 milliseconds with the enzyme).<sup id="cite_ref-Radzicka1995_63-0" class="reference"><a href="#cite_note-Radzicka1995-63"><span class="cite-bracket">[</span>63<span class="cite-bracket">]</span></a></sup> </p><p>The molecules bound and acted upon by enzymes are called <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrates</a>. Although enzymes can consist of hundreds of amino acids, it is usually only a small fraction of the residues that come in contact with the substrate, and an even smaller fraction—three to four residues on average—that are directly involved in catalysis.<sup id="cite_ref-urlEBI_64-0" class="reference"><a href="#cite_note-urlEBI-64"><span class="cite-bracket">[</span>64<span class="cite-bracket">]</span></a></sup> The region of the enzyme that binds the substrate and contains the catalytic residues is known as the <a href="/wiki/Active_site" title="Active site">active site</a>.<sup id="cite_ref-Biochemistry2010_54-3" class="reference"><a href="#cite_note-Biochemistry2010-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 389">: 389 </span></sup> </p><p><a href="/wiki/Dirigent_protein" title="Dirigent protein">Dirigent proteins</a> are members of a class of proteins that dictate the <a href="/wiki/Stereochemistry" title="Stereochemistry">stereochemistry</a> of a compound synthesized by other enzymes.<sup id="cite_ref-Pickel_2013_65-0" class="reference"><a href="#cite_note-Pickel_2013-65"><span class="cite-bracket">[</span>65<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Cell_signaling_and_ligand_binding">Cell signaling and ligand binding</h3></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/Glycan-protein_interactions" title="Glycan-protein interactions">Glycan-protein interactions</a></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Mouse_cholera_antibody.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a2/Mouse_cholera_antibody.png/170px-Mouse_cholera_antibody.png" decoding="async" width="170" height="227" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a2/Mouse_cholera_antibody.png/255px-Mouse_cholera_antibody.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a2/Mouse_cholera_antibody.png/340px-Mouse_cholera_antibody.png 2x" data-file-width="900" data-file-height="1200" /></a><figcaption><a href="/wiki/Ribbon_diagram" title="Ribbon diagram">Ribbon diagram</a> of a mouse antibody against <a href="/wiki/Cholera" title="Cholera">cholera</a> that binds a <a href="/wiki/Carbohydrate" title="Carbohydrate">carbohydrate</a> antigen</figcaption></figure> <p>Many proteins are involved in the process of <a href="/wiki/Cell_signaling" title="Cell signaling">cell signaling</a> and <a href="/wiki/Signal_transduction" title="Signal transduction">signal transduction</a>. Some proteins, such as <a href="/wiki/Insulin" title="Insulin">insulin</a>, are extracellular proteins that transmit a signal from the cell in which they were synthesized to other cells in distant <a href="/wiki/Biological_tissue" class="mw-redirect" title="Biological tissue">tissues</a>. Others are <a href="/wiki/Membrane_protein" title="Membrane protein">membrane proteins</a> that act as <a href="/wiki/Receptor_(biochemistry)" title="Receptor (biochemistry)">receptors</a> whose main function is to bind a signaling molecule and induce a biochemical response in the cell. Many receptors have a binding site exposed on the cell surface and an effector domain within the cell, which may have enzymatic activity or may undergo a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a> detected by other proteins within the cell.<sup id="cite_ref-Brandon_1999_41-1" class="reference"><a href="#cite_note-Brandon_1999-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 251–81">: 251–81 </span></sup> </p><p><a href="/wiki/Antibodies" class="mw-redirect" title="Antibodies">Antibodies</a> are protein components of an <a href="/wiki/Adaptive_immune_system" title="Adaptive immune system">adaptive immune system</a> whose main function is to bind <a href="/wiki/Antigen" title="Antigen">antigens</a>, or foreign substances in the body, and target them for destruction. Antibodies can be <a href="/wiki/Secrete" class="mw-redirect" title="Secrete">secreted</a> into the extracellular environment or anchored in the membranes of specialized <a href="/wiki/B_cell" title="B cell">B cells</a> known as <a href="/wiki/Plasma_cell" title="Plasma cell">plasma cells</a>. Whereas enzymes are limited in their binding affinity for their substrates by the necessity of conducting their reaction, antibodies have no such constraints. An antibody's binding affinity to its target is extraordinarily high.<sup id="cite_ref-Van_Holde_1996_42-6" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 275–50">: 275–50 </span></sup> </p><p>Many ligand transport proteins bind particular <a href="/wiki/Small_molecule" title="Small molecule">small biomolecules</a> and transport them to other locations in the body of a multicellular organism. These proteins must have a high binding affinity when their <a href="/wiki/Ligand" title="Ligand">ligand</a> is present in high concentrations, and release the ligand when it is present at low concentrations in the target tissues. The canonical example of a ligand-binding protein is <a href="/wiki/Haemoglobin" class="mw-redirect" title="Haemoglobin">haemoglobin</a>, which transports <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> from the <a href="/wiki/Lung" title="Lung">lungs</a> to other organs and tissues in all <a href="/wiki/Vertebrate" title="Vertebrate">vertebrates</a> and has close homologs in every biological <a href="/wiki/Kingdom_(biology)" title="Kingdom (biology)">kingdom</a>.<sup id="cite_ref-Van_Holde_1996_42-7" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 222–29">: 222–29 </span></sup> <a href="/wiki/Lectins" class="mw-redirect" title="Lectins">Lectins</a> are <a href="/wiki/Glycan-protein_interactions" title="Glycan-protein interactions">sugar-binding proteins</a> which are highly specific for their sugar moieties. <a href="/wiki/Lectins" class="mw-redirect" title="Lectins">Lectins</a> typically play a role in biological <a href="/wiki/Molecular_recognition" title="Molecular recognition">recognition</a> phenomena involving cells and proteins.<sup id="cite_ref-Rudiger2000_66-0" class="reference"><a href="#cite_note-Rudiger2000-66"><span class="cite-bracket">[</span>66<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Receptor_(biochemistry)" title="Receptor (biochemistry)">Receptors</a> and <a href="/wiki/Hormone" title="Hormone">hormones</a> are highly specific binding proteins. </p><p><a href="/wiki/Transmembrane_protein" title="Transmembrane protein">Transmembrane proteins</a> can serve as ligand transport proteins that alter the <a href="/wiki/Semipermeable_membrane" title="Semipermeable membrane">permeability</a> of the cell membrane to <a href="/wiki/Small_molecule" title="Small molecule">small molecules</a> and ions. The membrane alone has a <a href="/wiki/Hydrophobic" class="mw-redirect" title="Hydrophobic">hydrophobic</a> core through which <a href="/wiki/Chemical_polarity" title="Chemical polarity">polar</a> or charged molecules cannot <a href="/wiki/Diffusion" title="Diffusion">diffuse</a>. Membrane proteins contain internal channels that allow such molecules to enter and exit the cell. Many <a href="/wiki/Ion_channel" title="Ion channel">ion channel</a> proteins are specialized to select for only a particular ion; for example, <a href="/wiki/Potassium" title="Potassium">potassium</a> and <a href="/wiki/Sodium" title="Sodium">sodium</a> channels often discriminate for only one of the two ions.<sup id="cite_ref-Brandon_1999_41-2" class="reference"><a href="#cite_note-Brandon_1999-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 232–34">: 232–34 </span></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Structural_proteins">Structural proteins</h3></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:CHOP_protein_structure.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/1/1c/CHOP_protein_structure.png/220px-CHOP_protein_structure.png" decoding="async" width="220" height="154" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/1c/CHOP_protein_structure.png/330px-CHOP_protein_structure.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/1c/CHOP_protein_structure.png/440px-CHOP_protein_structure.png 2x" data-file-width="3000" data-file-height="2100" /></a><figcaption>Protein Structure</figcaption></figure> <p>Structural proteins confer stiffness and rigidity to otherwise-fluid biological components. Most structural proteins are <a href="/wiki/Fibrous_protein" title="Fibrous protein">fibrous proteins</a>; for example, <a href="/wiki/Collagen" title="Collagen">collagen</a> and <a href="/wiki/Elastin" title="Elastin">elastin</a> are critical components of <a href="/wiki/Connective_tissue" title="Connective tissue">connective tissue</a> such as <a href="/wiki/Cartilage" title="Cartilage">cartilage</a>, and <a href="/wiki/Keratin" title="Keratin">keratin</a> is found in hard or filamentous structures such as <a href="/wiki/Hair" title="Hair">hair</a>, <a href="/wiki/Nail_(anatomy)" title="Nail (anatomy)">nails</a>, <a href="/wiki/Feather" title="Feather">feathers</a>, <a href="/wiki/Hoof" title="Hoof">hooves</a>, and some <a href="/wiki/Exoskeleton" title="Exoskeleton">animal shells</a>.<sup id="cite_ref-Van_Holde_1996_42-8" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 178–81">: 178–81 </span></sup> Some <a href="/wiki/Globular_proteins" class="mw-redirect" title="Globular proteins">globular proteins</a> can play structural functions, for example, <a href="/wiki/Actin" title="Actin">actin</a> and <a href="/wiki/Tubulin" title="Tubulin">tubulin</a> are globular and soluble as monomers, but <a href="/wiki/Polymer" title="Polymer">polymerize</a> to form long, stiff fibers that make up the <a href="/wiki/Cytoskeleton" title="Cytoskeleton">cytoskeleton</a>, which allows the cell to maintain its shape and size.<sup id="cite_ref-Biochemistry2010_54-4" class="reference"><a href="#cite_note-Biochemistry2010-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 490">: 490 </span></sup> </p><p>Other proteins that serve structural functions are <a href="/wiki/Motor_protein" title="Motor protein">motor proteins</a> such as <a href="/wiki/Myosin" title="Myosin">myosin</a>, <a href="/wiki/Kinesin" title="Kinesin">kinesin</a>, and <a href="/wiki/Dynein" title="Dynein">dynein</a>, which are capable of generating mechanical forces. These proteins are crucial for cellular <a href="/wiki/Motility" title="Motility">motility</a> of single celled organisms and the <a href="/wiki/Spermatozoon" title="Spermatozoon">sperm</a> of many multicellular organisms which reproduce <a href="/wiki/Sexual_reproduction" title="Sexual reproduction">sexually</a>. They generate the forces exerted by contracting <a href="/wiki/Muscle" title="Muscle">muscles</a><sup id="cite_ref-Van_Holde_1996_42-9" class="reference"><a href="#cite_note-Van_Holde_1996-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 258–64, 272">: 258–64, 272 </span></sup> and play essential roles in intracellular transport.<sup id="cite_ref-Biochemistry2010_54-5" class="reference"><a href="#cite_note-Biochemistry2010-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 481, 490">: 481, 490 </span></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Methods_of_study">Methods of study</h2></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_methods" title="Protein methods">Protein methods</a></div> <p>Methods commonly used to study protein structure and function include <a href="/wiki/Immunohistochemistry" title="Immunohistochemistry">immunohistochemistry</a>, <a href="/wiki/Site-directed_mutagenesis" title="Site-directed mutagenesis">site-directed mutagenesis</a>, <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a>, <a href="/wiki/Nuclear_magnetic_resonance" title="Nuclear magnetic resonance">nuclear magnetic resonance</a> and <a href="/wiki/Mass_spectrometry" title="Mass spectrometry">mass spectrometry</a>. The activities and structures of proteins may be examined <i><a href="/wiki/In_vitro" title="In vitro">in vitro</a>,</i> <i><a href="/wiki/In_vivo" title="In vivo">in vivo</a>, and <a href="/wiki/In_silico" title="In silico">in silico</a></i>. <i><b>In vitro</b></i> studies of purified proteins in controlled environments are useful for learning how a protein carries out its function:<sup id="cite_ref-67" class="reference"><a href="#cite_note-67"><span class="cite-bracket">[</span>67<span class="cite-bracket">]</span></a></sup> for example, <a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">enzyme kinetics</a> studies explore the <a href="/wiki/Reaction_mechanism" title="Reaction mechanism">chemical mechanism</a> of an enzyme's catalytic activity and its relative affinity for various possible substrate molecules.<sup id="cite_ref-68" class="reference"><a href="#cite_note-68"><span class="cite-bracket">[</span>68<span class="cite-bracket">]</span></a></sup> By contrast, <i><b>in vivo</b></i> experiments can provide information about the physiological role of a protein in the context of a <a href="/wiki/Cell_biology" title="Cell biology">cell</a> or even a whole <a href="/wiki/Organism" title="Organism">organism</a>, and can often provide more information about protein behavior in different contexts.<sup id="cite_ref-69" class="reference"><a href="#cite_note-69"><span class="cite-bracket">[</span>69<span class="cite-bracket">]</span></a></sup> <i><b>In silico</b></i> studies use computational methods to study proteins.<sup id="cite_ref-70" class="reference"><a href="#cite_note-70"><span class="cite-bracket">[</span>70<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Protein_purification">Protein purification</h3></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_purification" title="Protein purification">Protein purification</a></div> <p>Proteins may be <a href="/wiki/Protein_purification" title="Protein purification">purified</a> from other cellular components using a variety of techniques such as <a href="/wiki/Ultracentrifugation" class="mw-redirect" title="Ultracentrifugation">ultracentrifugation</a>, <a href="/wiki/Precipitation_(chemistry)" title="Precipitation (chemistry)">precipitation</a>, <a href="/wiki/Electrophoresis" title="Electrophoresis">electrophoresis</a>, and <a href="/wiki/Chromatography" title="Chromatography">chromatography</a>;<sup id="cite_ref-Murray_2006_36-5" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 21–24">: 21–24 </span></sup> the advent of <a href="/wiki/Genetic_engineering" title="Genetic engineering">genetic engineering</a> has made possible a number of methods to facilitate purification.<sup id="cite_ref-Terpe2003_71-0" class="reference"><a href="#cite_note-Terpe2003-71"><span class="cite-bracket">[</span>71<span class="cite-bracket">]</span></a></sup> </p><p>To perform <i><a href="/wiki/In_vitro" title="In vitro">in vitro</a></i> analysis, a protein must be purified away from other cellular components. This process usually begins with <a href="/wiki/Cytolysis" title="Cytolysis">cell lysis</a>, in which a cell's membrane is disrupted and its internal contents released into a solution known as a <a href="/wiki/Crude_lysate" class="mw-redirect" title="Crude lysate">crude lysate</a>. The resulting mixture can be purified using <a href="/wiki/Ultracentrifugation" class="mw-redirect" title="Ultracentrifugation">ultracentrifugation</a>, which fractionates the various cellular components into fractions containing soluble proteins; membrane <a href="/wiki/Lipid" title="Lipid">lipids</a> and proteins; cellular <a href="/wiki/Organelle" title="Organelle">organelles</a>, and <a href="/wiki/Nucleic_acid" title="Nucleic acid">nucleic acids</a>. <a href="/wiki/Precipitation_(chemistry)" title="Precipitation (chemistry)">Precipitation</a> by a method known as <a href="/wiki/Salting_out" title="Salting out">salting out</a> can concentrate the proteins from this lysate. Various types of <a href="/wiki/Chromatography" title="Chromatography">chromatography</a> are then used to isolate the protein or proteins of interest based on properties such as molecular weight, net charge and binding affinity.<sup id="cite_ref-Murray_2006_36-6" class="reference"><a href="#cite_note-Murray_2006-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 21–24">: 21–24 </span></sup> The level of purification can be monitored using various types of <a href="/wiki/Gel_electrophoresis" title="Gel electrophoresis">gel electrophoresis</a> if the desired protein's molecular weight and <a href="/wiki/Isoelectric_point" title="Isoelectric point">isoelectric point</a> are known, by <a href="/wiki/Spectroscopy" title="Spectroscopy">spectroscopy</a> if the protein has distinguishable spectroscopic features, or by <a href="/wiki/Enzyme_assay" title="Enzyme assay">enzyme assays</a> if the protein has enzymatic activity. Additionally, proteins can be isolated according to their charge using <a href="/wiki/Electrofocusing" class="mw-redirect" title="Electrofocusing">electrofocusing</a>.<sup id="cite_ref-Hey2008_72-0" class="reference"><a href="#cite_note-Hey2008-72"><span class="cite-bracket">[</span>72<span class="cite-bracket">]</span></a></sup> </p><p>For natural proteins, a series of purification steps may be necessary to obtain protein sufficiently pure for laboratory applications. To simplify this process, <a href="/wiki/Genetic_engineering" title="Genetic engineering">genetic engineering</a> is often used to add chemical features to proteins that make them easier to purify without affecting their structure or activity. Here, a "tag" consisting of a specific amino acid sequence, often a series of <a href="/wiki/Histidine" title="Histidine">histidine</a> residues (a "<a href="/wiki/His-tag" title="His-tag">His-tag</a>"), is attached to one terminus of the protein. As a result, when the lysate is passed over a chromatography column containing <a href="/wiki/Nickel" title="Nickel">nickel</a>, the histidine residues ligate the nickel and attach to the column while the untagged components of the lysate pass unimpeded. A number of tags have been developed to help researchers purify specific proteins from complex mixtures.<sup id="cite_ref-Terpe2003_71-1" class="reference"><a href="#cite_note-Terpe2003-71"><span class="cite-bracket">[</span>71<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Cellular_localization">Cellular localization</h3></div> <figure class="mw-default-size mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Localisations02eng.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6e/Localisations02eng.jpg/300px-Localisations02eng.jpg" decoding="async" width="300" height="395" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6e/Localisations02eng.jpg/450px-Localisations02eng.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/6/6e/Localisations02eng.jpg 2x" data-file-width="469" data-file-height="618" /></a><figcaption>Proteins in various <a href="/wiki/Cellular_compartment" title="Cellular compartment">cellular compartments</a> and structures tagged with <a href="/wiki/Green_fluorescent_protein" title="Green fluorescent protein">green fluorescent protein</a> (here, white)</figcaption></figure> <p>The study of proteins <i>in vivo</i> is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a> and membrane-bound or secreted proteins in the <a href="/wiki/Endoplasmic_reticulum" title="Endoplasmic reticulum">endoplasmic reticulum</a>, the specifics of how proteins are <a href="/wiki/Protein_targeting" title="Protein targeting">targeted</a> to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a <a href="/wiki/Fusion_protein" title="Fusion protein">fusion protein</a> or <a href="/wiki/Chimera_(protein)" class="mw-redirect" title="Chimera (protein)">chimera</a> consisting of the natural protein of interest linked to a "<a href="/wiki/Reporter_gene" title="Reporter gene">reporter</a>" such as <a href="/wiki/Green_fluorescent_protein" title="Green fluorescent protein">green fluorescent protein</a> (GFP).<sup id="cite_ref-Stepanenko2008_73-0" class="reference"><a href="#cite_note-Stepanenko2008-73"><span class="cite-bracket">[</span>73<span class="cite-bracket">]</span></a></sup> The fused protein's position within the cell can then be cleanly and efficiently visualized using <a href="/wiki/Microscopy" title="Microscopy">microscopy</a>.<sup id="cite_ref-Yuste2005_74-0" class="reference"><a href="#cite_note-Yuste2005-74"><span class="cite-bracket">[</span>74<span class="cite-bracket">]</span></a></sup> </p><p>Other methods for elucidating the cellular location of proteins requires the use of known compartmental markers for regions such as the ER, the Golgi, lysosomes or vacuoles, mitochondria, chloroplasts, plasma membrane, etc. With the use of fluorescently tagged versions of these markers or of antibodies to known markers, it becomes much simpler to identify the localization of a protein of interest. For example, <a href="/wiki/Indirect_immunofluorescence" class="mw-redirect" title="Indirect immunofluorescence">indirect immunofluorescence</a> will allow for fluorescence colocalization and demonstration of location. Fluorescent dyes are used to label cellular compartments for a similar purpose.<sup id="cite_ref-Margolin2000_75-0" class="reference"><a href="#cite_note-Margolin2000-75"><span class="cite-bracket">[</span>75<span class="cite-bracket">]</span></a></sup> </p><p>Other possibilities exist, as well. For example, <a href="/wiki/Immunohistochemistry" title="Immunohistochemistry">immunohistochemistry</a> usually uses an antibody to one or more proteins of interest that are conjugated to enzymes yielding either luminescent or chromogenic signals that can be compared between samples, allowing for localization information.<sup id="cite_ref-76" class="reference"><a href="#cite_note-76"><span class="cite-bracket">[</span>76<span class="cite-bracket">]</span></a></sup> Another applicable technique is cofractionation in sucrose (or other material) gradients using <a href="/wiki/Isopycnic_centrifugation" class="mw-redirect" title="Isopycnic centrifugation">isopycnic centrifugation</a>.<sup id="cite_ref-Walker2000_77-0" class="reference"><a href="#cite_note-Walker2000-77"><span class="cite-bracket">[</span>77<span class="cite-bracket">]</span></a></sup> While this technique does not prove colocalization of a compartment of known density and the protein of interest, it indicates an increased likelihood.<sup id="cite_ref-Walker2000_77-1" class="reference"><a href="#cite_note-Walker2000-77"><span class="cite-bracket">[</span>77<span class="cite-bracket">]</span></a></sup> </p><p>Finally, the gold-standard method of cellular localization is <a href="/wiki/Immunoelectron_microscopy" class="mw-redirect" title="Immunoelectron microscopy">immunoelectron microscopy</a>. This technique uses an antibody to the protein of interest, along with classical electron microscopy techniques. The sample is prepared for normal electron microscopic examination, and then treated with an antibody to the protein of interest that is conjugated to an extremely electro-dense material, usually gold. This allows for the localization of both ultrastructural details as well as the protein of interest.<sup id="cite_ref-Mayhew2008_78-0" class="reference"><a href="#cite_note-Mayhew2008-78"><span class="cite-bracket">[</span>78<span class="cite-bracket">]</span></a></sup> </p><p>Through another genetic engineering application known as <a href="/wiki/Site-directed_mutagenesis" title="Site-directed mutagenesis">site-directed mutagenesis</a>, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation. This technique even allows the incorporation of unnatural amino acids into proteins, using modified tRNAs,<sup id="cite_ref-Hohsaka2002_79-0" class="reference"><a href="#cite_note-Hohsaka2002-79"><span class="cite-bracket">[</span>79<span class="cite-bracket">]</span></a></sup> and may allow the rational <a href="/wiki/Protein_design" title="Protein design">design</a> of new proteins with novel properties.<sup id="cite_ref-Cedrone2000_80-0" class="reference"><a href="#cite_note-Cedrone2000-80"><span class="cite-bracket">[</span>80<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Proteomics">Proteomics</h3></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/Proteomics" title="Proteomics">Proteomics</a></div> <p>The total complement of proteins present at a time in a cell or cell type is known as its <a href="/wiki/Proteome" title="Proteome">proteome</a>, and the study of such large-scale data sets defines the field of <a href="/wiki/Proteomics" title="Proteomics">proteomics</a>, named by analogy to the related field of <a href="/wiki/Genomics" title="Genomics">genomics</a>. Key experimental techniques in proteomics include <a href="/wiki/Two-dimensional_gel_electrophoresis" title="Two-dimensional gel electrophoresis">2D electrophoresis</a>,<sup id="cite_ref-Gorg2008_81-0" class="reference"><a href="#cite_note-Gorg2008-81"><span class="cite-bracket">[</span>81<span class="cite-bracket">]</span></a></sup> which allows the separation of many proteins, <a href="/wiki/Mass_spectrometry" title="Mass spectrometry">mass spectrometry</a>,<sup id="cite_ref-Conrotto2008_82-0" class="reference"><a href="#cite_note-Conrotto2008-82"><span class="cite-bracket">[</span>82<span class="cite-bracket">]</span></a></sup> which allows rapid high-throughput identification of proteins and sequencing of peptides (most often after <a href="/wiki/In-gel_digestion" title="In-gel digestion">in-gel digestion</a>), <a href="/wiki/Protein_microarray" title="Protein microarray">protein microarrays</a>, which allow the detection of the relative levels of the various proteins present in a cell, and <a href="/wiki/Two-hybrid_screening" title="Two-hybrid screening">two-hybrid screening</a>, which allows the systematic exploration of <a href="/wiki/Protein%E2%80%93protein_interaction" title="Protein–protein interaction">protein–protein interactions</a>.<sup id="cite_ref-Koegl2007_83-0" class="reference"><a href="#cite_note-Koegl2007-83"><span class="cite-bracket">[</span>83<span class="cite-bracket">]</span></a></sup> The total complement of biologically possible such interactions is known as the <a href="/wiki/Interactome" title="Interactome">interactome</a>.<sup id="cite_ref-Plewczynski2009_84-0" class="reference"><a href="#cite_note-Plewczynski2009-84"><span class="cite-bracket">[</span>84<span class="cite-bracket">]</span></a></sup> A systematic attempt to determine the structures of proteins representing every possible fold is known as <a href="/wiki/Structural_genomics" title="Structural genomics">structural genomics</a>.<sup id="cite_ref-Zhang2003_85-0" class="reference"><a href="#cite_note-Zhang2003-85"><span class="cite-bracket">[</span>85<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Structure_determination">Structure determination</h3></div> <p>Discovering the tertiary structure of a protein, or the quaternary structure of its complexes, can provide important clues about how the protein performs its function and how it can be affected, i.e. in <a href="/wiki/Drug_design#Structure-based" title="Drug design">drug design</a>. As proteins are <a href="/wiki/Diffraction-limited_system" title="Diffraction-limited system">too small to be seen</a> under a <a href="/wiki/Optical_microscope" title="Optical microscope">light microscope</a>, other methods have to be employed to determine their structure. Common experimental methods include <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a> and <a href="/wiki/Protein_NMR" class="mw-redirect" title="Protein NMR">NMR spectroscopy</a>, both of which can produce structural information at <a href="/wiki/Atom" title="Atom">atomic</a> resolution. However, NMR experiments are able to provide information from which a subset of distances between pairs of atoms can be estimated, and the final possible conformations for a protein are determined by solving a <a href="/wiki/Distance_geometry" title="Distance geometry">distance geometry</a> problem. <a href="/wiki/Dual_polarisation_interferometry" class="mw-redirect" title="Dual polarisation interferometry">Dual polarisation interferometry</a> is a quantitative analytical method for measuring the overall <a href="/wiki/Protein_conformation" class="mw-redirect" title="Protein conformation">protein conformation</a> and <a href="/wiki/Conformational_change" title="Conformational change">conformational changes</a> due to interactions or other stimulus. <a href="/wiki/Circular_dichroism" title="Circular dichroism">Circular dichroism</a> is another laboratory technique for determining internal β-sheet / α-helical composition of proteins. <a href="/wiki/Cryoelectron_microscopy" class="mw-redirect" title="Cryoelectron microscopy">Cryoelectron microscopy</a> is used to produce lower-resolution structural information about very large protein complexes, including assembled <a href="/wiki/Virus" title="Virus">viruses</a>;<sup id="cite_ref-Brandon_1999_41-3" class="reference"><a href="#cite_note-Brandon_1999-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup><sup class="reference nowrap"><span title="Page / location: 340–41">: 340–41 </span></sup> a variant known as <a href="/wiki/Electron_crystallography" title="Electron crystallography">electron crystallography</a> can produce high-resolution information in some cases, especially for two-dimensional crystals of membrane proteins.<sup id="cite_ref-Gonen2005_86-0" class="reference"><a href="#cite_note-Gonen2005-86"><span class="cite-bracket">[</span>86<span class="cite-bracket">]</span></a></sup> Solved structures are usually deposited in the <a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">Protein Data Bank</a> (PDB), a freely available resource from which structural data about thousands of proteins can be obtained in the form of <a href="/wiki/Cartesian_coordinates" class="mw-redirect" title="Cartesian coordinates">Cartesian coordinates</a> for each atom in the protein.<sup id="cite_ref-Standley2008_87-0" class="reference"><a href="#cite_note-Standley2008-87"><span class="cite-bracket">[</span>87<span class="cite-bracket">]</span></a></sup> </p><p>Many more gene sequences are known than protein structures. Further, the set of solved structures is biased toward proteins that can be easily subjected to the conditions required in <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a>, one of the major structure determination methods. In particular, globular proteins are comparatively easy to <a href="/wiki/Crystallize" class="mw-redirect" title="Crystallize">crystallize</a> in preparation for X-ray crystallography. Membrane proteins and large protein complexes, by contrast, are difficult to crystallize and are underrepresented in the PDB.<sup id="cite_ref-Walian2004_88-0" class="reference"><a href="#cite_note-Walian2004-88"><span class="cite-bracket">[</span>88<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Structural_genomics" title="Structural genomics">Structural genomics</a> initiatives have attempted to remedy these deficiencies by systematically solving representative structures of major fold classes. <a href="/wiki/Protein_structure_prediction" title="Protein structure prediction">Protein structure prediction</a> methods attempt to provide a means of generating a plausible structure for proteins whose structures have not been experimentally determined.<sup id="cite_ref-Sleator2012_89-0" class="reference"><a href="#cite_note-Sleator2012-89"><span class="cite-bracket">[</span>89<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Structure_prediction">Structure prediction</h3></div> <figure class="mw-default-size mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:225_Peptide_Bond-01.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/2/26/225_Peptide_Bond-01.jpg/350px-225_Peptide_Bond-01.jpg" decoding="async" width="350" height="297" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/26/225_Peptide_Bond-01.jpg/525px-225_Peptide_Bond-01.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/26/225_Peptide_Bond-01.jpg/700px-225_Peptide_Bond-01.jpg 2x" data-file-width="2219" data-file-height="1886" /></a><figcaption>Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure, in this case hemoglobin containing <a href="/wiki/Heme" title="Heme">heme</a> units</figcaption></figure> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main articles: <a href="/wiki/Protein_structure_prediction" title="Protein structure prediction">Protein structure prediction</a> and <a href="/wiki/List_of_protein_structure_prediction_software" title="List of protein structure prediction software">List of protein structure prediction software</a></div> <p>Complementary to the field of structural genomics, <i>protein structure prediction</i> develops efficient <a href="/wiki/Mathematical_model" title="Mathematical model">mathematical models</a> of proteins to computationally predict the molecular formations in theory, instead of detecting structures with laboratory observation.<sup id="cite_ref-Zhang2008_90-0" class="reference"><a href="#cite_note-Zhang2008-90"><span class="cite-bracket">[</span>90<span class="cite-bracket">]</span></a></sup> The most successful type of structure prediction, known as <a href="/wiki/Homology_modeling" title="Homology modeling">homology modeling</a>, relies on the existence of a "template" structure with sequence similarity to the protein being modeled; structural genomics' goal is to provide sufficient representation in solved structures to model most of those that remain.<sup id="cite_ref-Xiang2006_91-0" class="reference"><a href="#cite_note-Xiang2006-91"><span class="cite-bracket">[</span>91<span class="cite-bracket">]</span></a></sup> Although producing accurate models remains a challenge when only distantly related template structures are available, it has been suggested that <a href="/wiki/Sequence_alignment" title="Sequence alignment">sequence alignment</a> is the bottleneck in this process, as quite accurate models can be produced if a "perfect" sequence alignment is known.<sup id="cite_ref-Zhang2005_92-0" class="reference"><a href="#cite_note-Zhang2005-92"><span class="cite-bracket">[</span>92<span class="cite-bracket">]</span></a></sup> Many structure prediction methods have served to inform the emerging field of <a href="/wiki/Protein_engineering" title="Protein engineering">protein engineering</a>, in which novel protein folds have already been designed.<sup id="cite_ref-Kuhlman2003_93-0" class="reference"><a href="#cite_note-Kuhlman2003-93"><span class="cite-bracket">[</span>93<span class="cite-bracket">]</span></a></sup> Many proteins (in eukaryotes ~33%) contain large unstructured but biologically functional segments and can be classified as <a href="/wiki/Intrinsically_disordered_proteins" title="Intrinsically disordered proteins">intrinsically disordered proteins</a>. Predicting and analysing protein disorder is an important part of protein structure characterisation.<sup id="cite_ref-94" class="reference"><a href="#cite_note-94"><span class="cite-bracket">[</span>94<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="In_silico_simulation_of_dynamical_processes">In silico simulation of dynamical processes</h3></div> <p>A more complex computational problem is the prediction of intermolecular interactions, such as in <a href="/wiki/Docking_(molecular)" title="Docking (molecular)">molecular docking</a>,<sup id="cite_ref-Ritchie2008_95-0" class="reference"><a href="#cite_note-Ritchie2008-95"><span class="cite-bracket">[</span>95<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Protein_folding" title="Protein folding">protein folding</a>, <a href="/wiki/Protein%E2%80%93protein_interaction" title="Protein–protein interaction">protein–protein interaction</a> and chemical reactivity. Mathematical models to simulate these dynamical processes involve <a href="/wiki/Molecular_mechanics" title="Molecular mechanics">molecular mechanics</a>, in particular, <a href="/wiki/Molecular_dynamics" title="Molecular dynamics">molecular dynamics</a>. In this regard, <i><a href="/wiki/In_silico" title="In silico">in silico</a></i> simulations discovered the folding of small α-helical <a href="/wiki/Protein_domain" title="Protein domain">protein domains</a> such as the <a href="/wiki/Villin" class="mw-redirect" title="Villin">villin</a> headpiece,<sup id="cite_ref-Zagrovic2002_96-0" class="reference"><a href="#cite_note-Zagrovic2002-96"><span class="cite-bracket">[</span>96<span class="cite-bracket">]</span></a></sup> the <a href="/wiki/HIV" title="HIV">HIV</a> accessory protein<sup id="cite_ref-Herges2005_97-0" class="reference"><a href="#cite_note-Herges2005-97"><span class="cite-bracket">[</span>97<span class="cite-bracket">]</span></a></sup> and hybrid methods combining standard molecular dynamics with <a href="/wiki/Quantum_mechanics" title="Quantum mechanics">quantum mechanical</a> mathematics have explored the electronic states of <a href="/wiki/Rhodopsin" title="Rhodopsin">rhodopsins</a>.<sup id="cite_ref-Hoffman2006_98-0" class="reference"><a href="#cite_note-Hoffman2006-98"><span class="cite-bracket">[</span>98<span class="cite-bracket">]</span></a></sup> </p><p>Beyond classical molecular dynamics, <a href="/wiki/Quantum_dynamics" title="Quantum dynamics">quantum dynamics</a> methods allow the simulation of proteins in atomistic detail with an accurate description of quantum mechanical effects. Examples include the multi-layer <a href="/wiki/Multi-configuration_time-dependent_Hartree" title="Multi-configuration time-dependent Hartree">multi-configuration time-dependent Hartree </a> method and the <a href="/wiki/Hierarchical_equations_of_motion" title="Hierarchical equations of motion">hierarchical equations of motion</a> approach, which have been applied to plant cryptochromes<sup id="cite_ref-Gatti2018_99-0" class="reference"><a href="#cite_note-Gatti2018-99"><span class="cite-bracket">[</span>99<span class="cite-bracket">]</span></a></sup> and bacteria light-harvesting complexes,<sup id="cite_ref-Schulten2012_100-0" class="reference"><a href="#cite_note-Schulten2012-100"><span class="cite-bracket">[</span>100<span class="cite-bracket">]</span></a></sup> respectively. Both quantum and classical mechanical simulations of biological-scale systems are extremely computationally demanding, so <a href="/wiki/Distributed_computing" title="Distributed computing">distributed computing</a> initiatives such as the <a href="/wiki/Folding@home" title="Folding@home">Folding@home</a> project facilitate the <a href="/wiki/Molecular_modeling_on_GPU" class="mw-redirect" title="Molecular modeling on GPU">molecular modeling</a> by exploiting advances in <a href="/wiki/Graphics_processing_unit" title="Graphics processing unit">GPU</a> parallel processing and <a href="/wiki/Monte_Carlo_method" title="Monte Carlo method">Monte Carlo</a> techniques.<sup id="cite_ref-Scheraga2007_101-0" class="reference"><a href="#cite_note-Scheraga2007-101"><span class="cite-bracket">[</span>101<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Zheng_Javidpour_2020_102-0" class="reference"><a href="#cite_note-Zheng_Javidpour_2020-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Chemical_analysis">Chemical analysis</h3></div> <p>The total nitrogen content of organic matter is mainly formed by the amino groups in proteins. The Total Kjeldahl Nitrogen (<a href="/wiki/TKN" class="mw-redirect" title="TKN">TKN</a>) is a measure of nitrogen widely used in the analysis of (waste) water, soil, food, feed and organic matter in general. As the name suggests, the <a href="/wiki/Kjeldahl_method" title="Kjeldahl method">Kjeldahl method</a> is applied. More sensitive methods are available.<sup id="cite_ref-103" class="reference"><a href="#cite_note-103"><span class="cite-bracket">[</span>103<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-104" class="reference"><a href="#cite_note-104"><span class="cite-bracket">[</span>104<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Digestion">Digestion</h2></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/Proteolysis" title="Proteolysis">Proteolysis</a></div> <figure class="skin-invert-image" typeof="mw:File/Thumb"><a href="/wiki/File:Proteolysis_scheme.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/8/80/Proteolysis_scheme.svg/230px-Proteolysis_scheme.svg.png" decoding="async" width="230" height="143" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/80/Proteolysis_scheme.svg/345px-Proteolysis_scheme.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/80/Proteolysis_scheme.svg/460px-Proteolysis_scheme.svg.png 2x" data-file-width="397" data-file-height="247" /></a><figcaption>Hydrolysis of protein. X = HCl and heat for industrial proteolysis. X = protease for biological proteolysis</figcaption></figure> <p>In the absence of catalysts, proteins are slow to <a href="/wiki/Hydrolysis" title="Hydrolysis">hydrolyze</a>.<sup id="cite_ref-Radzicka_Wolfenden_1996_105-0" class="reference"><a href="#cite_note-Radzicka_Wolfenden_1996-105"><span class="cite-bracket">[</span>105<span class="cite-bracket">]</span></a></sup> The breakdown of proteins to small peptides and amino acids (<a href="/wiki/Proteolysis" title="Proteolysis">proteolysis</a>) is a step in <a href="/wiki/Digestion" title="Digestion">digestion</a>; these breakdown products are then absorbed in the small intestine.<sup id="cite_ref-Keller_2013_106-0" class="reference"><a href="#cite_note-Keller_2013-106"><span class="cite-bracket">[</span>106<span class="cite-bracket">]</span></a></sup> The hydrolysis of proteins relies on enzymes called <a href="/wiki/Protease" title="Protease">proteases</a> or peptidases. Proteases, which are themselves proteins, come in several types according to the particular <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a> that they cleave as well as their tendency to cleave peptide bonds at the terminus of a protein (exopeptidases) vs peptide bonds at the interior of the protein (endopeptidases).<sup id="cite_ref-107" class="reference"><a href="#cite_note-107"><span class="cite-bracket">[</span>107<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Pepsin" title="Pepsin">Pepsin</a> is an endopeptidase in the stomach. Subsequent to the stomach, the pancreas secretes other proteases to complete the hydrolysis, these include <a href="/wiki/Trypsin" title="Trypsin">trypsin</a> and <a href="/wiki/Chymotrypsin" title="Chymotrypsin">chymotrypsin</a>.<sup id="cite_ref-Switzar_Giera_2013_108-0" class="reference"><a href="#cite_note-Switzar_Giera_2013-108"><span class="cite-bracket">[</span>108<span class="cite-bracket">]</span></a></sup> </p><p>Protein hydrolysis is employed commercially as a means of producing amino acids from bulk sources of protein, such as blood meal, feathers, keratin. Such materials are treated with hot <a href="/wiki/Hydrochloric_acid" title="Hydrochloric acid">hydrochloric acid</a>, which effects the hydrolysis of the peptide bonds.<sup id="cite_ref-109" class="reference"><a href="#cite_note-109"><span class="cite-bracket">[</span>109<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Mechanical_properties">Mechanical properties</h2></div> <p>The <a href="/wiki/Mechanical_properties_of_biomaterials" title="Mechanical properties of biomaterials">mechanical properties</a> of proteins are highly diverse and are often central to their biological function, as in the case of proteins like <a href="/wiki/Keratin" title="Keratin">keratin</a> and <a href="/wiki/Collagen" title="Collagen">collagen</a>.<sup id="cite_ref-110" class="reference"><a href="#cite_note-110"><span class="cite-bracket">[</span>110<span class="cite-bracket">]</span></a></sup> For instance, the ability of <a href="/wiki/Muscle" title="Muscle">muscle tissue</a> to continually expand and contract is directly tied to the elastic properties of their underlying protein makeup.<sup id="cite_ref-111" class="reference"><a href="#cite_note-111"><span class="cite-bracket">[</span>111<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-112" class="reference"><a href="#cite_note-112"><span class="cite-bracket">[</span>112<span class="cite-bracket">]</span></a></sup> Beyond fibrous proteins, the conformational dynamics of <a href="/wiki/Enzyme" title="Enzyme">enzymes</a><sup id="cite_ref-113" class="reference"><a href="#cite_note-113"><span class="cite-bracket">[</span>113<span class="cite-bracket">]</span></a></sup> and the structure of <a href="/wiki/Biological_membrane" title="Biological membrane">biological membranes</a>, among other biological functions, are governed by the mechanical properties of the proteins. Outside of their biological context, the unique mechanical properties of many proteins, along with their relative sustainability when compared to <a href="/wiki/List_of_synthetic_polymers" title="List of synthetic polymers">synthetic polymers</a>, have made them desirable targets for next-generation materials design.<sup id="cite_ref-114" class="reference"><a href="#cite_note-114"><span class="cite-bracket">[</span>114<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-115" class="reference"><a href="#cite_note-115"><span class="cite-bracket">[</span>115<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Young%27s_modulus" title="Young's modulus">Young's modulus</a>, <i>E,</i> is calculated as the axial stress σ over the resulting strain ε. It is a measure of the relative <a href="/wiki/Stiffness" title="Stiffness">stiffness</a> of a material. In the context of proteins, this stiffness often directly correlates to biological function. For example, <a href="/wiki/Collagen" title="Collagen">collagen</a>, found in <a href="/wiki/Connective_tissue" title="Connective tissue">connective tissue</a>, <a href="/wiki/Bone" title="Bone">bones</a>, and <a href="/wiki/Cartilage" title="Cartilage">cartilage</a>, and <a href="/wiki/Keratin" title="Keratin">keratin</a>, found in nails, claws, and hair, have observed stiffnesses that are several orders of magnitude higher than that of <a href="/wiki/Elastin" title="Elastin">elastin</a>,<sup id="cite_ref-Guthold-2007_116-0" class="reference"><a href="#cite_note-Guthold-2007-116"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup> which is though to give elasticity to structures such as <a href="/wiki/Blood_vessel" title="Blood vessel">blood vessels</a>, <a href="/wiki/Lung" title="Lung">pulmonary tissue</a>, and <a href="/wiki/Bladder" title="Bladder">bladder tissue</a>, among others.<sup id="cite_ref-117" class="reference"><a href="#cite_note-117"><span class="cite-bracket">[</span>117<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-118" class="reference"><a href="#cite_note-118"><span class="cite-bracket">[</span>118<span class="cite-bracket">]</span></a></sup> In comparison to this, <a href="/wiki/Globular_protein" title="Globular protein">globular proteins</a>, such as <a href="/wiki/Bovine_serum_albumin" title="Bovine serum albumin">Bovine Serum Albumin</a>, which float relatively freely in the <a href="/wiki/Cytosol" title="Cytosol">cytosol</a> and often function as enzymes (and thus undergoing frequent conformational changes) have comparably much lower Young's moduli.<sup id="cite_ref-Khoury-2019_119-0" class="reference"><a href="#cite_note-Khoury-2019-119"><span class="cite-bracket">[</span>119<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-120" class="reference"><a href="#cite_note-120"><span class="cite-bracket">[</span>120<span class="cite-bracket">]</span></a></sup> </p><p>The Young's modulus of a single protein can be found through <a href="/wiki/Molecular_dynamics" title="Molecular dynamics">molecular dynamics</a> simulation. Using either atomistic force-fields, such as <a href="/wiki/CHARMM" title="CHARMM">CHARMM</a> or <a href="/wiki/GROMOS" title="GROMOS">GROMOS</a>, or coarse-grained forcefields like Martini,<sup id="cite_ref-121" class="reference"><a href="#cite_note-121"><span class="cite-bracket">[</span>121<span class="cite-bracket">]</span></a></sup> a single protein molecule can be stretched by a uniaxial force while the resulting extension is recorded in order to calculate the strain.<sup id="cite_ref-122" class="reference"><a href="#cite_note-122"><span class="cite-bracket">[</span>122<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-123" class="reference"><a href="#cite_note-123"><span class="cite-bracket">[</span>123<span class="cite-bracket">]</span></a></sup> Experimentally, methods such as <a href="/wiki/Atomic_force_microscopy" title="Atomic force microscopy">atomic force microscopy</a> can be used to obtain similar data.<sup id="cite_ref-124" class="reference"><a href="#cite_note-124"><span class="cite-bracket">[</span>124<span class="cite-bracket">]</span></a></sup> </p><p>At the macroscopic level, the Young's modulus of cross-linked protein networks can be obtained through more traditional <a href="/wiki/Mechanical_testing" title="Mechanical testing">mechanical testing</a>. Experimentally observed values for a few proteins can be seen below. </p> <table class="wikitable"> <caption>Elasticity of Various Proteins </caption> <tbody><tr> <th>Protein </th> <th>Protein Class </th> <th>Young's modulus </th></tr> <tr> <td>Keratin (Cross-Linked) </td> <td>Fibrous </td> <td>1.5-10 GPa<sup id="cite_ref-125" class="reference"><a href="#cite_note-125"><span class="cite-bracket">[</span>125<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Elastin (Cross-Linked) </td> <td>Fibrous </td> <td>1 MPa<sup id="cite_ref-Guthold-2007_116-1" class="reference"><a href="#cite_note-Guthold-2007-116"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Fibrin (Cross-linked) </td> <td>Fibrous </td> <td>1-10 MPa <sup id="cite_ref-Guthold-2007_116-2" class="reference"><a href="#cite_note-Guthold-2007-116"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Collagen (Cross-linked) </td> <td>Fibrous </td> <td>5-7.5 GPa<sup id="cite_ref-Guthold-2007_116-3" class="reference"><a href="#cite_note-Guthold-2007-116"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-126" class="reference"><a href="#cite_note-126"><span class="cite-bracket">[</span>126<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Resilin (Cross-Linked) </td> <td>Fibrous </td> <td>1-2 MPa<sup id="cite_ref-Guthold-2007_116-4" class="reference"><a href="#cite_note-Guthold-2007-116"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Bovine Serum Albumin (Cross-Linked) </td> <td>Globular </td> <td>2.5-15 KPa<sup id="cite_ref-Khoury-2019_119-1" class="reference"><a href="#cite_note-Khoury-2019-119"><span class="cite-bracket">[</span>119<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>β-Barrel Outer Membrane Proteins </td> <td>Membrane </td> <td>20-45 GPa<sup id="cite_ref-127" class="reference"><a href="#cite_note-127"><span class="cite-bracket">[</span>127<span class="cite-bracket">]</span></a></sup> </td></tr></tbody></table> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2></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" style="column-width: 30em;"> <ul><li><a href="/wiki/Deproteination" title="Deproteination">Deproteination</a></li> <li><a href="/wiki/DNA-binding_protein" title="DNA-binding protein">DNA-binding protein</a></li> <li><a href="/wiki/Macromolecule" title="Macromolecule">Macromolecule</a></li> <li><a href="/wiki/Index_of_protein-related_articles" title="Index of protein-related articles">Index of protein-related articles</a></li> <li><a href="/wiki/Intein" class="mw-redirect" title="Intein">Intein</a></li> <li><a href="/wiki/List_of_proteins" title="List of proteins">List of proteins</a></li> <li><a href="/wiki/Proteopathy" class="mw-redirect" title="Proteopathy">Proteopathy</a></li> <li><a href="/wiki/Proteopedia" title="Proteopedia">Proteopedia</a></li> <li><a href="/wiki/Sequence_space_(evolution)" title="Sequence space (evolution)">Protein sequence space</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Protein superfamily</a></li> <li><a href="/wiki/Molecular_evolution" title="Molecular evolution">Protein evolution</a></li></ul></div><div style="clear:both;" class=""></div> <div class="mw-heading mw-heading2"><h2 id="References">References</h2></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 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.id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output 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title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=Atomic+force+microscopy+captures+length+phenotypes+in+single+proteins&rft.volume=96&rft.issue=20&rft.pages=%3Cspan+class%3D%22nowrap%22%3E11288-%3C%2Fspan%3E11292&rft.date=1999-09&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC18026%23id-name%3DPMC&rft_id=info%3Apmid%2F10500169&rft_id=info%3Adoi%2F10.1073%2Fpnas.96.20.11288&rft_id=info%3Abibcode%2F1999PNAS...9611288C&rft.aulast=Carrion-Vazquez&rft.aufirst=M&rft.au=Marszalek%2C+PE&rft.au=Oberhauser%2C+AF&rft.au=Fernandez%2C+JM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC18026&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></span> </li> <li id="cite_note-125"><span class="mw-cite-backlink"><b><a href="#cite_ref-125">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMcKittrickChenBoddeYang2012" class="citation journal cs1">McKittrick J, Chen PY, Bodde SG, Yang W, Novitskaya EE, Meyers MA (2012-04-03). <a rel="nofollow" class="external text" href="http://link.springer.com/10.1007/s11837-012-0302-8">"The Structure, Functions, and Mechanical Properties of Keratin"</a>. <i>JOM</i>. <b>64</b> (4): <span class="nowrap">449–</span>468. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2012JOM....64d.449M">2012JOM....64d.449M</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs11837-012-0302-8">10.1007/s11837-012-0302-8</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=JOM&rft.atitle=The+Structure%2C+Functions%2C+and+Mechanical+Properties+of+Keratin&rft.volume=64&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E449-%3C%2Fspan%3E468&rft.date=2012-04-03&rft_id=info%3Adoi%2F10.1007%2Fs11837-012-0302-8&rft_id=info%3Abibcode%2F2012JOM....64d.449M&rft.aulast=McKittrick&rft.aufirst=J&rft.au=Chen%2C+PY&rft.au=Bodde%2C+SG&rft.au=Yang%2C+W&rft.au=Novitskaya%2C+EE&rft.au=Meyers%2C+MA&rft_id=http%3A%2F%2Flink.springer.com%2F10.1007%2Fs11837-012-0302-8&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></span> </li> <li id="cite_note-126"><span class="mw-cite-backlink"><b><a href="#cite_ref-126">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFYangvan_der_WerfFitiéBennink2008" class="citation journal cs1">Yang L, van der Werf KO, Fitié CF, Bennink ML, Dijkstra PJ, Feijen J (March 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2257912">"Mechanical properties of native and cross-linked type I collagen fibrils"</a>. <i>Biophysical Journal</i>. <b>94</b> (6): <span class="nowrap">2204–</span>2211. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2008BpJ....94.2204Y">2008BpJ....94.2204Y</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1529%2Fbiophysj.107.111013">10.1529/biophysj.107.111013</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2257912">2257912</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18032556">18032556</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biophysical+Journal&rft.atitle=Mechanical+properties+of+native+and+cross-linked+type+I+collagen+fibrils&rft.volume=94&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2204-%3C%2Fspan%3E2211&rft.date=2008-03&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2257912%23id-name%3DPMC&rft_id=info%3Apmid%2F18032556&rft_id=info%3Adoi%2F10.1529%2Fbiophysj.107.111013&rft_id=info%3Abibcode%2F2008BpJ....94.2204Y&rft.aulast=Yang&rft.aufirst=L&rft.au=van+der+Werf%2C+KO&rft.au=Fiti%C3%A9%2C+CF&rft.au=Bennink%2C+ML&rft.au=Dijkstra%2C+PJ&rft.au=Feijen%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2257912&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></span> </li> <li id="cite_note-127"><span class="mw-cite-backlink"><b><a href="#cite_ref-127">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFLessenFlemingFlemingSodt2018" class="citation journal cs1">Lessen HJ, Fleming PJ, Fleming KG, Sodt AJ (August 2018). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6191857">"Building Blocks of the Outer Membrane: Calculating a General Elastic Energy Model for β-Barrel Membrane Proteins"</a>. <i>Journal of Chemical Theory and Computation</i>. <b>14</b> (8): <span class="nowrap">4487–</span>4497. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Facs.jctc.8b00377">10.1021/acs.jctc.8b00377</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6191857">6191857</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29979594">29979594</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Chemical+Theory+and+Computation&rft.atitle=Building+Blocks+of+the+Outer+Membrane%3A+Calculating+a+General+Elastic+Energy+Model+for+%CE%B2-Barrel+Membrane+Proteins&rft.volume=14&rft.issue=8&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4487-%3C%2Fspan%3E4497&rft.date=2018-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6191857%23id-name%3DPMC&rft_id=info%3Apmid%2F29979594&rft_id=info%3Adoi%2F10.1021%2Facs.jctc.8b00377&rft.aulast=Lessen&rft.aufirst=HJ&rft.au=Fleming%2C+PJ&rft.au=Fleming%2C+KG&rft.au=Sodt%2C+AJ&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6191857&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2></div> <dl><dt>Textbooks</dt></dl> <style data-mw-deduplicate="TemplateStyles:r1239549316">.mw-parser-output .refbegin{margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}@media screen{.mw-parser-output .refbegin{font-size:90%}}</style><div class="refbegin refbegin-columns references-column-width" style="column-width: 32em"> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite class="citation book cs1">Branden C, Tooze J (1999). <i>Introduction to Protein Structure</i>. New York: Garland Pub. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-8153-2305-1" title="Special:BookSources/978-0-8153-2305-1"><bdi>978-0-8153-2305-1</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Introduction+to+Protein+Structure&rft.place=New+York&rft.pub=Garland+Pub&rft.date=1999&rft.isbn=978-0-8153-2305-1&rft.aulast=Branden&rft.aufirst=C&rft.au=Tooze%2C+J&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite class="citation book cs1">Murray RF, Harper HW, Granner DK, Mayes PA, Rodwell VW (2006). <i>Harper's Illustrated Biochemistry</i>. New York: Lange Medical Books/McGraw-Hill. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-07-146197-9" title="Special:BookSources/978-0-07-146197-9"><bdi>978-0-07-146197-9</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Harper%27s+Illustrated+Biochemistry&rft.place=New+York&rft.pub=Lange+Medical+Books%2FMcGraw-Hill&rft.date=2006&rft.isbn=978-0-07-146197-9&rft.aulast=Murray&rft.aufirst=RF&rft.au=Harper%2C+HW&rft.au=Granner%2C+DK&rft.au=Mayes%2C+PA&rft.au=Rodwell%2C+VW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite class="citation book cs1">Van Holde KE, Mathews CK (1996). <a rel="nofollow" class="external text" href="https://archive.org/details/biochemistry00math"><i>Biochemistry</i></a>. Menlo Park, California: Benjamin/Cummings Pub. Co., Inc. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-8053-3931-4" title="Special:BookSources/978-0-8053-3931-4"><bdi>978-0-8053-3931-4</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Biochemistry&rft.place=Menlo+Park%2C+California&rft.pub=Benjamin%2FCummings+Pub.+Co.%2C+Inc&rft.date=1996&rft.isbn=978-0-8053-3931-4&rft.aulast=Van+Holde&rft.aufirst=KE&rft.au=Mathews%2C+CK&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fbiochemistry00math&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></li></ul> </div> <dl><dt>History</dt></dl> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite class="citation book cs1">Tanford C, Reynolds JA (2001). <i>Nature's Robots: A History of Proteins</i>. Oxford New York: Oxford University Press, USA. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-19-850466-5" title="Special:BookSources/978-0-19-850466-5"><bdi>978-0-19-850466-5</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Nature%27s+Robots%3A+A+History+of+Proteins&rft.place=Oxford+New+York&rft.pub=Oxford+University+Press%2C+USA&rft.date=2001&rft.isbn=978-0-19-850466-5&rft.aulast=Tanford&rft.aufirst=Charles&rft.au=Reynolds%2C+Jacqueline+Ann&rfr_id=info%3Asid%2Fen.wikipedia.org%3AProtein" class="Z3988"></span></li></ul> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2></div> <style data-mw-deduplicate="TemplateStyles:r1235681985">.mw-parser-output .side-box{margin:4px 0;box-sizing:border-box;border:1px solid #aaa;font-size:88%;line-height:1.25em;background-color:var(--background-color-interactive-subtle,#f8f9fa);display:flow-root}.mw-parser-output .side-box-abovebelow,.mw-parser-output .side-box-text{padding:0.25em 0.9em}.mw-parser-output .side-box-image{padding:2px 0 2px 0.9em;text-align:center}.mw-parser-output .side-box-imageright{padding:2px 0.9em 2px 0;text-align:center}@media(min-width:500px){.mw-parser-output .side-box-flex{display:flex;align-items:center}.mw-parser-output .side-box-text{flex:1;min-width:0}}@media(min-width:720px){.mw-parser-output .side-box{width:238px}.mw-parser-output .side-box-right{clear:right;float:right;margin-left:1em}.mw-parser-output .side-box-left{margin-right:1em}}</style><style data-mw-deduplicate="TemplateStyles:r1250146164">.mw-parser-output .sister-box .side-box-abovebelow{padding:0.75em 0;text-align:center}.mw-parser-output .sister-box .side-box-abovebelow>b{display:block}.mw-parser-output .sister-box .side-box-text>ul{border-top:1px solid #aaa;padding:0.75em 0;width:217px;margin:0 auto}.mw-parser-output .sister-box .side-box-text>ul>li{min-height:31px}.mw-parser-output .sister-logo{display:inline-block;width:31px;line-height:31px;vertical-align:middle;text-align:center}.mw-parser-output .sister-link{display:inline-block;margin-left:4px;width:182px;vertical-align:middle}@media print{body.ns-0 .mw-parser-output .sistersitebox{display:none!important}}@media screen{html.skin-theme-clientpref-night .mw-parser-output .sistersitebox img[src*="Wiktionary-logo-v2.svg"]{background-color:white}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .sistersitebox img[src*="Wiktionary-logo-v2.svg"]{background-color:white}}</style><div role="navigation" aria-labelledby="sister-projects" class="side-box metadata side-box-right sister-box sistersitebox plainlinks"><style data-mw-deduplicate="TemplateStyles:r1126788409">.mw-parser-output .plainlist ol,.mw-parser-output .plainlist ul{line-height:inherit;list-style:none;margin:0;padding:0}.mw-parser-output .plainlist ol li,.mw-parser-output .plainlist ul li{margin-bottom:0}</style> <div class="side-box-abovebelow"> <b>Protein</b> at Wikipedia's <a href="/wiki/Wikipedia:Wikimedia_sister_projects" title="Wikipedia:Wikimedia sister projects"><span id="sister-projects">sister projects</span></a></div> <div class="side-box-flex"> <div class="side-box-text plainlist"><ul><li><span class="sister-logo"><span class="mw-valign-middle" typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/0/06/Wiktionary-logo-v2.svg/27px-Wiktionary-logo-v2.svg.png" decoding="async" width="27" height="27" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/0/06/Wiktionary-logo-v2.svg/41px-Wiktionary-logo-v2.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/0/06/Wiktionary-logo-v2.svg/54px-Wiktionary-logo-v2.svg.png 2x" data-file-width="391" data-file-height="391" /></span></span></span><span class="sister-link"><a href="https://en.wiktionary.org/wiki/protein" class="extiw" title="wikt:protein">Definitions</a> from Wiktionary</span></li><li><span class="sister-logo"><span class="mw-valign-middle" typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/20px-Commons-logo.svg.png" decoding="async" width="20" height="27" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/30px-Commons-logo.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/40px-Commons-logo.svg.png 2x" data-file-width="1024" data-file-height="1376" /></span></span></span><span class="sister-link"><a href="https://commons.wikimedia.org/wiki/Category:Proteins" class="extiw" title="c:Category:Proteins">Media</a> from Commons</span></li></ul></div></div> </div> <div class="mw-heading mw-heading3"><h3 id="Databases_and_projects">Databases and projects</h3></div> <ul><li><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=protein">NCBI Entrez Protein database</a></li> <li><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=structure">NCBI Protein Structure database</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20060424071622/http://www.hprd.org/">Human Protein Reference Database</a></li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20070314135408/http://www.humanproteinpedia.org/">Human Proteinpedia</a></li> <li><a rel="nofollow" class="external text" href="http://folding.stanford.edu/">Folding@Home (Stanford University)</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20120908075542/http://folding.stanford.edu/English/HomePage">Archived</a> 2012-09-08 at the <a href="/wiki/Wayback_Machine" title="Wayback Machine">Wayback Machine</a></li> <li><a rel="nofollow" class="external text" href="http://www.pdbe.org/">Protein Databank in Europe</a> (see also <a rel="nofollow" class="external text" href="https://archive.today/20130727184433/http://www.pdbe.org/quips">PDBeQuips</a>, short articles and tutorials on interesting PDB structures)</li> <li><a rel="nofollow" class="external text" href="http://www.rcsb.org/">Research Collaboratory for Structural Bioinformatics</a> (see also <a rel="nofollow" class="external text" href="http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html">Molecule of the Month</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20200724151351/https://www.rcsb.org/pdb/static.do?p=education_discussion%2Fmolecule_of_the_month%2Findex.html">Archived</a> 2020-07-24 at the <a href="/wiki/Wayback_Machine" title="Wayback Machine">Wayback Machine</a>, presenting short accounts on selected proteins from the PDB)</li> <li><a rel="nofollow" class="external text" href="http://www.proteopedia.org/">Proteopedia – Life in 3D</a>: rotatable, zoomable 3D model with wiki annotations for every known protein molecular structure.</li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20080608183902/http://www.expasy.uniprot.org/">UniProt the Universal Protein Resource</a></li></ul> <div class="mw-heading mw-heading3"><h3 id="Tutorials_and_educational_websites">Tutorials and educational websites</h3></div> <ul><li><a rel="nofollow" class="external text" href="https://web.stanford.edu/group/hopes/cgi-bin/hopes_test/an-introduction-to-proteins/">"An Introduction to Proteins"</a> from <a href="/wiki/HOPES" class="mw-redirect" title="HOPES">HOPES</a> (Huntington's Disease Outreach Project for Education at Stanford)</li> <li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20050219090405/http://www.biochemweb.org/proteins.shtml">Proteins: Biogenesis to Degradation – The Virtual Library of Biochemistry and 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.navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Gene_expression217" style="padding:3px"><table class="nowraplinks hlist mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" 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abbr{color:var(--color-base)!important}@media(prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}}@media print{.mw-parser-output .navbar{display:none!important}}</style><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Gene_expression" title="Template:Gene expression"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Gene_expression" title="Template talk:Gene expression"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Gene_expression" title="Special:EditPage/Template:Gene expression"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Gene_expression217" style="font-size:114%;margin:0 4em"><a href="/wiki/Gene_expression" title="Gene expression">Gene expression</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Introduction_to_genetics" title="Introduction to genetics">Introduction<br />to genetics</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Genetic_code" title="Genetic code">Genetic code</a></li> <li><a href="/wiki/Central_dogma_of_molecular_biology" title="Central dogma of molecular biology">Central dogma</a> <ul><li><a href="/wiki/DNA" title="DNA">DNA</a> → <a href="/wiki/Messenger_RNA" title="Messenger RNA">RNA</a> → <a class="mw-selflink selflink">Protein</a></li></ul></li> <li><a href="/wiki/Central_dogma_of_molecular_biology#Special_transfers_of_biological_sequential_information" title="Central dogma of molecular biology">Special transfers</a> <ul><li><a href="/wiki/RNA-dependent_RNA_polymerase" title="RNA-dependent RNA polymerase">RNA→RNA</a></li> <li><a href="/wiki/Reverse_transcription" class="mw-redirect" title="Reverse transcription">RNA→DNA</a></li> <li><a href="/wiki/Prion" title="Prion">Protein→Protein</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Transcription_(biology)" title="Transcription (biology)">Transcription</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Types</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bacterial_transcription" title="Bacterial transcription">Bacterial</a></li> <li><a href="/wiki/Archaeal_transcription" title="Archaeal transcription">Archaeal</a></li> <li><a href="/wiki/Eukaryotic_transcription" title="Eukaryotic transcription">Eukaryotic</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Key elements</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Transcription_factor" title="Transcription factor">Transcription factor</a></li> <li><a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a></li> <li><a href="/wiki/Promoter_(genetics)" title="Promoter (genetics)">Promoter</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;"><a href="/wiki/Post-transcriptional_modification" title="Post-transcriptional modification">Post-transcription</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Primary_transcript" title="Primary transcript">Precursor mRNA (pre-mRNA / hnRNA)</a></li> <li><a href="/wiki/Five-prime_cap" title="Five-prime cap">5' capping</a></li> <li><a href="/wiki/RNA_splicing" title="RNA splicing">Splicing</a></li> <li><a href="/wiki/Polyadenylation" title="Polyadenylation">Polyadenylation</a></li> <li><a href="/wiki/Histone_acetylation_and_deacetylation" title="Histone acetylation and deacetylation">Histone acetylation and deacetylation</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Translation_(biology)" title="Translation (biology)">Translation</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Types</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bacterial_translation" title="Bacterial translation">Bacterial</a></li> <li><a href="/wiki/Archaeal_translation" title="Archaeal translation">Archaeal</a></li> <li><a href="/wiki/Eukaryotic_translation" title="Eukaryotic translation">Eukaryotic</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Key elements</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0;white-space:nowrap;"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Ribosome" title="Ribosome">Ribosome</a></li> <li><a href="/wiki/Transfer_RNA" title="Transfer RNA">Transfer RNA (tRNA)</a></li> <li><a href="/wiki/Ribosome-nascent_chain_complex" title="Ribosome-nascent chain complex">Ribosome-nascent chain complex (RNC)</a></li> <li><a href="/wiki/Post-translational_modification" title="Post-translational modification">Post-translational modification</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Regulation_of_gene_expression" title="Regulation of gene expression">Regulation</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Epigenetics" title="Epigenetics">Epigenetic</a> <ul><li><a href="/wiki/Genomic_imprinting" title="Genomic imprinting">imprinting</a></li></ul></li> <li><a href="/wiki/Transcriptional_regulation" title="Transcriptional regulation">Transcriptional</a> <ul><li><a href="/wiki/Gene_regulatory_network" title="Gene regulatory network">Gene regulatory network</a></li> <li><a href="/wiki/Cis-regulatory_element" title="Cis-regulatory element">cis-regulatory element</a></li></ul></li> <li><a href="/wiki/Lac_operon" title="Lac operon">lac operon</a></li> <li><a href="/wiki/Post-transcriptional_regulation" title="Post-transcriptional regulation">Post-transcriptional</a> <ul><li><a href="/wiki/P-bodies" title="P-bodies">sequestration (P-bodies)</a></li> <li><a href="/wiki/Alternative_splicing" title="Alternative splicing">alternative splicing</a></li> <li><a href="/wiki/MicroRNA" title="MicroRNA">microRNA</a></li></ul></li> <li><a href="/wiki/Translational_regulation" title="Translational regulation">Translational</a></li> <li><a href="/wiki/Post-translational_regulation" title="Post-translational regulation">Post-translational</a> <ul><li><a href="/wiki/Phosphorylation" title="Phosphorylation">reversible</a></li> <li><a href="/wiki/Proteolysis" title="Proteolysis">irreversible</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Influential people</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Fran%C3%A7ois_Jacob" title="François Jacob">François Jacob</a></li> <li><a href="/wiki/Jacques_Monod" title="Jacques Monod">Jacques Monod</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="Proteins36" style="padding:3px"><table class="nowraplinks hlist mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><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:Protein_topics" title="Template:Protein topics"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Protein_topics" title="Template talk:Protein topics"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Protein_topics" title="Special:EditPage/Template:Protein topics"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Proteins36" style="font-size:114%;margin:0 4em"><a class="mw-selflink selflink">Proteins</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Processes</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein_biosynthesis" title="Protein biosynthesis">Protein biosynthesis</a></li> <li><a href="/wiki/Post-translational_modification" title="Post-translational modification">Post-translational modification</a></li> <li><a href="/wiki/Protein_folding" title="Protein folding">Protein folding</a></li> <li><a href="/wiki/Protein_targeting" title="Protein targeting">Protein targeting</a></li> <li><a href="/wiki/Proteome" title="Proteome">Proteome</a></li> <li><a href="/wiki/Protein_methods" title="Protein methods">Protein methods</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Structures</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein_structure" title="Protein structure">Protein structure</a></li> <li><a href="/wiki/Protein_domain" title="Protein domain">Protein structural domains</a></li> <li><a href="/wiki/Proteasome" title="Proteasome">Proteasome</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/List_of_proteins" title="List of proteins">List of proteins</a></li> <li><a href="/wiki/Membrane_protein" title="Membrane protein">Membrane protein</a></li> <li><a href="/wiki/Globular_protein" title="Globular protein">Globular protein</a> <ul><li><a href="/wiki/Globulin" title="Globulin">Globulin</a></li> <li><a href="/wiki/Edestin" title="Edestin">Edestin</a></li> <li><a href="/wiki/Albumin" title="Albumin">Albumin</a></li></ul></li> <li><a href="/wiki/Scleroprotein" class="mw-redirect" title="Scleroprotein">Fibrous protein</a></li> <li><a href="/wiki/Chromoprotein" title="Chromoprotein">Chromoprotein</a></li> <li><a href="/wiki/Photoreceptor_protein" title="Photoreceptor protein">Photoreceptor protein</a></li> <li><a href="/wiki/Biliprotein" title="Biliprotein">Biliprotein</a> <ul><li><a href="/wiki/Phycobiliprotein" title="Phycobiliprotein">Phycobiliprotein</a></li> <li><a href="/wiki/Phytochrome" title="Phytochrome">Phytochrome</a></li> <li><a href="/wiki/Lipocalin" title="Lipocalin">Lipocalin</a></li></ul></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="Proteins:_key_methods_of_study146" 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"><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:Protein_methods" title="Template:Protein methods"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Protein_methods" title="Template talk:Protein methods"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Protein_methods" title="Special:EditPage/Template:Protein methods"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Proteins:_key_methods_of_study146" style="font-size:114%;margin:0 4em"><a class="mw-selflink selflink">Proteins</a>: key <a href="/wiki/Protein_methods" title="Protein methods">methods</a> of study</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Experiment" title="Experiment">Experimental</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_purification" title="Protein purification">Protein purification</a></li> <li><a href="/wiki/Green_fluorescent_protein" title="Green fluorescent protein">Green fluorescent protein</a></li> <li><a href="/wiki/Western_blot" title="Western blot">Western blot</a></li> <li><a href="/wiki/Immunostaining" title="Immunostaining">Protein immunostaining</a></li> <li><a href="/wiki/Protein_sequencing" title="Protein sequencing">Protein sequencing</a></li> <li><a href="/wiki/Gel_electrophoresis" title="Gel electrophoresis">Gel electrophoresis</a>/<a href="/wiki/Gel_electrophoresis_of_proteins" title="Gel electrophoresis of proteins">Protein electrophoresis</a></li> <li><a href="/wiki/Immunoprecipitation" title="Immunoprecipitation">Protein immunoprecipitation</a></li> <li><a href="/wiki/Peptide_mass_fingerprinting" title="Peptide mass fingerprinting">Peptide mass fingerprinting</a>/<a href="/wiki/Protein_mass_spectrometry" title="Protein mass spectrometry">Protein mass spectrometry</a></li> <li><a href="/wiki/Dual-polarization_interferometry" title="Dual-polarization interferometry">Dual-polarization interferometry</a></li> <li><a href="/wiki/Microscale_thermophoresis" title="Microscale thermophoresis">Microscale thermophoresis</a></li> <li><a href="/wiki/Chromatin_immunoprecipitation" title="Chromatin immunoprecipitation">Chromatin immunoprecipitation</a></li> <li><a href="/wiki/Surface_plasmon_resonance" title="Surface plasmon resonance">Surface plasmon resonance</a></li> <li><a href="/wiki/Isothermal_titration_calorimetry" title="Isothermal titration calorimetry">Isothermal titration calorimetry</a></li> <li><a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a></li> <li><a href="/wiki/Nuclear_magnetic_resonance_spectroscopy_of_proteins" title="Nuclear magnetic resonance spectroscopy of proteins">Protein NMR</a></li> <li><a href="/wiki/Cryo-electron_microscopy" class="mw-redirect" title="Cryo-electron microscopy">Cryo-electron microscopy</a></li> <li><a href="/wiki/Electron_microscope#Sample_preparation" title="Electron microscope">Freeze-fracture electron microscopy</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Bioinformatics" title="Bioinformatics">Bioinformatics</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/Protein_structure_prediction" title="Protein structure prediction">Protein structure prediction</a></li> <li><a href="/wiki/Protein_function_prediction" title="Protein function prediction">Protein function prediction</a></li> <li><a href="/wiki/Macromolecular_docking" title="Macromolecular docking">Protein–protein docking</a></li> <li><a href="/wiki/Structural_alignment" title="Structural alignment">Protein structural alignment</a></li> <li><a href="/wiki/Gene_ontology" class="mw-redirect" title="Gene ontology">Protein ontology</a></li> <li><a href="/wiki/Protein%E2%80%93protein_interaction_prediction" title="Protein–protein interaction prediction">Protein–protein interaction prediction</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Assay" title="Assay">Assay</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/Enzyme_assay" title="Enzyme assay">Enzyme assay</a></li> <li><a href="/wiki/Bradford_protein_assay" title="Bradford protein assay">Protein assay</a></li> <li><a href="/wiki/Secretion_assay" title="Secretion assay">Secretion assay</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Display techniques</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/Bacterial_display" title="Bacterial display">Bacterial display</a></li> <li><a href="/wiki/MRNA_display" title="MRNA display">mRNA display</a></li> <li><a href="/wiki/Phage_display" title="Phage display">Phage display</a></li> <li><a href="/wiki/Ribosome_display" title="Ribosome display">Ribosome display</a></li> <li><a href="/wiki/Yeast_display" title="Yeast display">Yeast display</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Super-resolution_microscopy" title="Super-resolution microscopy">Super-resolution microscopy</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/Photoactivated_localization_microscopy" title="Photoactivated localization microscopy">Photoactivated localization microscopy</a></li> <li><a href="/wiki/Vertico_spatially_modulated_illumination" title="Vertico spatially modulated illumination">Vertico SMI</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="Food_chemistry18" 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"><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:Food_chemistry" title="Template:Food chemistry"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Food_chemistry" title="Template talk:Food chemistry"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Food_chemistry" title="Special:EditPage/Template:Food chemistry"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Food_chemistry18" style="font-size:114%;margin:0 4em"><a href="/wiki/Food_chemistry" title="Food chemistry">Food chemistry</a></div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Food_additive" title="Food additive">Additives</a></li> <li><a href="/wiki/Carbohydrate" title="Carbohydrate">Carbohydrates</a></li> <li><a href="/wiki/Food_coloring" title="Food coloring">Coloring</a></li> <li><a href="/wiki/Enzyme" title="Enzyme">Enzymes</a></li> <li><a href="/wiki/Essential_fatty_acid" title="Essential fatty acid">Essential fatty acids</a></li> <li><a href="/wiki/Flavoring" title="Flavoring">Flavors</a></li> <li><a href="/wiki/Food_fortification" title="Food fortification">Fortification</a></li> <li><a href="/wiki/Lipid" title="Lipid">Lipids</a></li> <li><a href="/wiki/Mineral_(nutrient)" title="Mineral (nutrient)">"Minerals" (Chemical elements)</a></li> <li><a class="mw-selflink selflink">Proteins</a></li> <li><a href="/wiki/Vitamin" title="Vitamin">Vitamins</a></li> <li><a href="/wiki/Water" title="Water">Water</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="Metabolism,_catabolism,_anabolism113" style="padding:3px"><table class="nowraplinks hlist mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><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:Metabolism" title="Template:Metabolism"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Metabolism" title="Template talk:Metabolism"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Metabolism" title="Special:EditPage/Template:Metabolism"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Metabolism,_catabolism,_anabolism113" style="font-size:114%;margin:0 4em"><a href="/wiki/Metabolism" title="Metabolism">Metabolism</a>, <a href="/wiki/Catabolism" title="Catabolism">catabolism</a>, <a href="/wiki/Anabolism" title="Anabolism">anabolism</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" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Metabolic_pathway" title="Metabolic pathway">Metabolic pathway</a></li> <li><a href="/wiki/Metabolic_network" title="Metabolic network">Metabolic network</a></li> <li><a href="/wiki/Primary_nutritional_groups" title="Primary nutritional groups">Primary nutritional groups</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Bioenergetics" title="Bioenergetics">Energy<br /> metabolism</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Aerobic_respiration" class="mw-redirect" title="Aerobic respiration">Aerobic respiration</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycolysis" title="Glycolysis">Glycolysis</a> → <a href="/wiki/Pyruvate_dehydrogenase" title="Pyruvate dehydrogenase">Pyruvate decarboxylation</a> → <a href="/wiki/Citric_acid_cycle" title="Citric acid cycle">Citric acid cycle</a> → <a href="/wiki/Oxidative_phosphorylation" title="Oxidative phosphorylation">Oxidative phosphorylation</a> (<span style="font-size:85%;"><a href="/wiki/Electron_transport_chain" title="Electron transport chain">electron transport chain</a> + <a href="/wiki/ATP_synthase" title="ATP synthase">ATP synthase</a></span>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Anaerobic_respiration" title="Anaerobic respiration">Anaerobic respiration</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>Electron acceptors other than oxygen</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Fermentation" title="Fermentation">Fermentation</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycolysis" title="Glycolysis">Glycolysis</a> → <a href="/wiki/Substrate-level_phosphorylation" title="Substrate-level phosphorylation">Substrate-level phosphorylation</a> <ul><li><a href="/wiki/Acetone%E2%80%93butanol%E2%80%93ethanol_fermentation" title="Acetone–butanol–ethanol fermentation">ABE</a></li> <li><a href="/wiki/Ethanol_fermentation" title="Ethanol fermentation">Ethanol</a></li> <li><a href="/wiki/Lactic_acid_fermentation" title="Lactic acid fermentation">Lactic acid</a></li></ul></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Specific<br /> paths</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Protein_metabolism" title="Protein metabolism">Protein metabolism</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein_biosynthesis" title="Protein biosynthesis">Protein synthesis</a></li> <li><a href="/wiki/Protein_catabolism" title="Protein catabolism">Catabolism</a> (protein→peptide→amino acid)</li></ul> </div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Amino_acid" title="Amino acid">Amino acid</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Amino_acid_synthesis" title="Amino acid synthesis">Amino acid synthesis</a></li> <li><a href="/wiki/Protein_catabolism#Amino_acid_degradation" title="Protein catabolism">Amino acid degradation</a> (amino acid→pyruvate, acetyl CoA, or TCA intermediate)</li> <li><a href="/wiki/Urea_cycle" title="Urea cycle">Urea cycle</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Nucleic_acid_metabolism" title="Nucleic acid metabolism">Nucleotide<br /> metabolism</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Purine_metabolism" title="Purine metabolism">Purine metabolism</a></li> <li><a href="/wiki/Nucleotide_salvage" title="Nucleotide salvage">Nucleotide salvage</a></li> <li><a href="/wiki/Pyrimidine_metabolism" title="Pyrimidine metabolism">Pyrimidine metabolism</a></li> <li><a href="/wiki/Purine_nucleotide_cycle" title="Purine nucleotide cycle">Purine nucleotide cycle</a></li></ul> </div></td></tr></tbody></table><div> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Carbohydrate_metabolism" title="Carbohydrate metabolism">Carbohydrate metabolism</a><br />(<a href="/wiki/Carbohydrate_catabolism" title="Carbohydrate catabolism">carbohydrate catabolism</a><br />and <a href="/wiki/Anabolism" title="Anabolism">anabolism</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">Human</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><td colspan="2" class="navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycolysis" title="Glycolysis">Glycolysis</a> ⇄ <a href="/wiki/Gluconeogenesis" title="Gluconeogenesis">Gluconeogenesis</a></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycogenolysis" title="Glycogenolysis">Glycogenolysis</a> ⇄ <a href="/wiki/Glycogenesis" title="Glycogenesis">Glycogenesis</a></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Pentose_phosphate_pathway" title="Pentose phosphate pathway">Pentose phosphate pathway</a></li> <li><a href="/wiki/Fructolysis" title="Fructolysis">Fructolysis</a> <ul><li><a href="/wiki/Polyol_pathway" title="Polyol pathway">Polyol pathway</a></li></ul></li> <li><a href="/wiki/Galactolysis" title="Galactolysis">Galactolysis</a> <ul><li><a href="/wiki/Leloir_pathway" title="Leloir pathway">Leloir pathway</a></li></ul></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycosylation" title="Glycosylation">Glycosylation</a> <ul><li><a href="/wiki/N-linked_glycosylation" title="N-linked glycosylation">N-linked</a></li> <li><a href="/wiki/O-linked_glycosylation" title="O-linked glycosylation">O-linked</a></li></ul></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Nonhuman</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><td colspan="2" class="navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Photosynthesis" title="Photosynthesis">Photosynthesis</a></li> <li><a href="/wiki/Anoxygenic_photosynthesis" title="Anoxygenic photosynthesis">Anoxygenic photosynthesis</a></li> <li><a href="/wiki/Chemosynthesis" title="Chemosynthesis">Chemosynthesis</a></li> <li><a href="/wiki/Carbon_fixation" class="mw-redirect" title="Carbon fixation">Carbon fixation</a></li> <li><a href="/w/index.php?title=DeLey-Doudoroff_pathway&action=edit&redlink=1" class="new" title="DeLey-Doudoroff pathway (page does not exist)">DeLey-Doudoroff pathway</a></li> <li><a href="/wiki/Entner-Doudoroff_pathway" class="mw-redirect" title="Entner-Doudoroff pathway">Entner-Doudoroff pathway</a></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Xylose_metabolism" title="Xylose metabolism">Xylose metabolism</a></li> <li><a href="/wiki/Radiotrophic_fungus" title="Radiotrophic fungus">Radiotrophism</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lipid_metabolism" title="Lipid metabolism">Lipid metabolism</a> <br />(<a href="/wiki/Lipolysis" title="Lipolysis">lipolysis</a>, <a href="/wiki/Lipogenesis" title="Lipogenesis">lipogenesis</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Fatty_acid_metabolism" title="Fatty acid metabolism">Fatty acid metabolism</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Fatty_acid_degradation" title="Fatty acid degradation">Fatty acid degradation</a> (<a href="/wiki/Beta_oxidation" title="Beta oxidation">Beta oxidation</a>)</li> <li><a href="/wiki/Fatty_acid_synthesis" title="Fatty acid synthesis">Fatty acid synthesis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Steroid" title="Steroid">Steroid metabolism</a></li> <li><a href="/wiki/Sphingolipid_metabolism" class="mw-redirect" title="Sphingolipid metabolism">Sphingolipid metabolism</a></li> <li><a href="/wiki/Eicosanoid_metabolism" class="mw-redirect" title="Eicosanoid metabolism">Eicosanoid metabolism</a></li> <li><a href="/wiki/Ketosis" title="Ketosis">Ketosis</a></li> <li><a href="/wiki/Reverse_cholesterol_transport" title="Reverse cholesterol transport">Reverse cholesterol transport</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bioinorganic_chemistry" title="Bioinorganic chemistry">Metal metabolism</a> <ul><li><a href="/wiki/Human_iron_metabolism" title="Human iron metabolism">Iron metabolism</a></li></ul></li> <li><a href="/wiki/Ethanol_metabolism" class="mw-redirect" title="Ethanol metabolism">Ethanol metabolism</a></li> <li><a href="/wiki/Phosphagen" title="Phosphagen">Phospagen system (ATP-PCr)</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table></div> <style data-mw-deduplicate="TemplateStyles:r1130092004">.mw-parser-output .portal-bar{font-size:88%;font-weight:bold;display:flex;justify-content:center;align-items:baseline}.mw-parser-output .portal-bar-bordered{padding:0 2em;background-color:#fdfdfd;border:1px solid #a2a9b1;clear:both;margin:1em auto 0}.mw-parser-output .portal-bar-related{font-size:100%;justify-content:flex-start}.mw-parser-output .portal-bar-unbordered{padding:0 1.7em;margin-left:0}.mw-parser-output .portal-bar-header{margin:0 1em 0 0.5em;flex:0 0 auto;min-height:24px}.mw-parser-output .portal-bar-content{display:flex;flex-flow:row wrap;flex:0 1 auto;padding:0.15em 0;column-gap:1em;align-items:baseline;margin:0;list-style:none}.mw-parser-output .portal-bar-content-related{margin:0;list-style:none}.mw-parser-output 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