{"id":3546,"date":"2020-09-23T07:41:15","date_gmt":"2020-09-23T06:41:15","guid":{"rendered":"https:\/\/ibb.uab.cat\/?p=3546"},"modified":"2020-09-23T07:44:28","modified_gmt":"2020-09-23T06:44:28","slug":"protein-folding-and-conformational-diseases-protocols-for-rational-design-of-protein-solubility-and-aggregation-properties-using-aggrescan3d-standalone","status":"publish","type":"post","link":"https:\/\/ibb.uab.cat\/index.php\/2020\/09\/23\/protein-folding-and-conformational-diseases-protocols-for-rational-design-of-protein-solubility-and-aggregation-properties-using-aggrescan3d-standalone\/","title":{"rendered":"Protein Folding and Conformational Diseases. &#8220;Protocols for rational design of protein solubility and aggregation properties using Aggrescan3D standalone&#8221;"},"content":{"rendered":"<h2 class=\"\"><img loading=\"lazy\" class=\"size-full wp-image-3547 alignleft\" src=\"https:\/\/ibb.uab.cat\/wp-content\/uploads\/F1.medium.gif\" alt=\"\" width=\"440\" height=\"415\" \/><\/h2>\n<div class=\"highwire-cite-title\">\n<div class=\"highwire-cite-title\">Protocols for rational design of protein solubility and aggregation properties using Aggrescan3D standalone<\/div>\n<\/div>\n<div class=\"highwire-cite-authors\"><span class=\"highwire-citation-authors\"><span class=\"highwire-citation-author first\" data-delta=\"0\"><span class=\"nlm-given-names\">Aleksander<\/span>\u00a0<span class=\"nlm-surname\">Kuriata<\/span><\/span>,\u00a0<span class=\"highwire-citation-author\" data-delta=\"1\"><span class=\"nlm-given-names\">Aleksandra E.<\/span>\u00a0<span class=\"nlm-surname\">Badaczewska-Dawid<\/span><\/span>,\u00a0<span class=\"highwire-citation-author\" data-delta=\"2\"><span class=\"nlm-given-names\">Jordi<\/span>\u00a0<span class=\"nlm-surname\">Pujols<\/span><\/span>,\u00a0<span class=\"highwire-citation-author\" data-delta=\"3\"><span class=\"nlm-given-names\">Salvador<\/span>\u00a0<span class=\"nlm-surname\">Ventura<\/span><\/span>,\u00a0<span class=\"highwire-citation-author\" data-delta=\"4\"><span class=\"nlm-given-names\">Sebastian<\/span>\u00a0<span class=\"nlm-surname\">Kmiecik<\/span><\/span><\/span><\/div>\n<div class=\"highwire-cite-metadata\"><span class=\"highwire-cite-metadata-journal highwire-cite-metadata\">bioRxiv\u00a0<\/span><span class=\"highwire-cite-metadata-pages highwire-cite-metadata\">2020.09.09.276915.<\/span><\/div>\n<div>\u00a0<\/div>\n<div class=\"highwire-cite-metadata\"><span class=\"highwire-cite-metadata-doi highwire-cite-metadata\"><span class=\"doi_label\">doi:<\/span>\u00a0https:\/\/doi.org\/10.1101\/2020.09.09.276915<\/span><\/div>\n<h4>https:\/\/www.biorxiv.org\/content\/10.1101\/2020.09.09.276915v1.full<\/h4>\n<h2 class=\"\" style=\"text-align: justify;\">Summary<\/h2>\n<p id=\"p-2\" style=\"text-align: justify;\">Protein aggregation is a major hurdle in the development and manufacturing of protein-based therapeutics. Development of aggregation-resistant and stable protein variants can be guided by rational redesign using computational tools. Here, we describe the architecture and functionalities of the Aggrescan3D (A3D) standalone package for the rational design of protein solubility and aggregation properties based on three-dimensional protein structures. We present the case studies of the three therapeutic proteins, including antibodies, exploring the practical use of the A3D standalone tool. The case studies demonstrate that protein solubility can be easily improved by the A3D prediction of non-destabilizing amino acid mutations at the protein surfaces.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Protocols for rational design of protein solubility and aggregation properties using Aggrescan3D standalone Aleksander\u00a0Kuriata,\u00a0Aleksandra E.\u00a0Badaczewska-Dawid,\u00a0Jordi\u00a0Pujols,\u00a0Salvador\u00a0Ventura,\u00a0Sebastian\u00a0Kmiecik bioRxiv\u00a02020.09.09.276915. \u00a0 doi:\u00a0https:\/\/doi.org\/10.1101\/2020.09.09.276915 https:\/\/www.biorxiv.org\/content\/10.1101\/2020.09.09.276915v1.full Summary Protein aggregation is a major hurdle in the development and manufacturing of protein-based therapeutics. Development of aggregation-resistant and stable protein variants can be guided by rational redesign using computational tools. Here, we describe the architecture [&hellip;]<\/p>\n","protected":false},"author":65,"featured_media":3548,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[4],"tags":[],"_links":{"self":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3546"}],"collection":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/users\/65"}],"replies":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/comments?post=3546"}],"version-history":[{"count":5,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3546\/revisions"}],"predecessor-version":[{"id":3553,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3546\/revisions\/3553"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media\/3548"}],"wp:attachment":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media?parent=3546"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/categories?post=3546"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/tags?post=3546"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}