http://debianws.lexgopc.com/wiki143/index.php?action=history&feed=atom&title=Intrinsically_disordered_proteins 2026-05-15T16:14:14Z Revision history for this page on the wiki MediaWiki 1.43.1 http://debianws.lexgopc.com/wiki143/index.php?title=Intrinsically_disordered_proteins&diff=2077711&oldid=prev 2025-06-24T08:23:31Z

<p><a href="https://en.wikipedia.org/wiki/OABOT" class="extiw" title="wikipedia:OABOT">Open access bot</a>: url-access=subscription updated in citation with #oabot.</p> <table style="background-color: #fff; color: #202122;" data-mw="interface"> <col class="diff-marker" /> <col class="diff-content" /> <col class="diff-marker" /> <col class="diff-content" /> <tr class="diff-title" lang="en"> <td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Previous revision</td> <td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:23, 24 June 2025</td> </tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l51">Line 51:</td> <td colspan="2" class="diff-lineno">Line 51:</td></tr> <tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Topological approaches have been developed to search for conformational patterns in their dynamics. For instance, [[circuit topology]] has been applied to track the dynamics of disordered protein domains.&lt;ref&gt;[https://pubs.acs.org/doi/10.1021/acs.jcim.3c00391 Scalvini B. et al., Circuit Topology Approach for the Comparative Analysis of Intrinsically Disordered Proteins. J. Chem. Inf. Model. 63, 8, 2586–2602 (2023)]&lt;/ref&gt; By employing a topological approach, one can categorize motifs according to their topological buildup and the timescale of their formation.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Topological approaches have been developed to search for conformational patterns in their dynamics. For instance, [[circuit topology]] has been applied to track the dynamics of disordered protein domains.&lt;ref&gt;[https://pubs.acs.org/doi/10.1021/acs.jcim.3c00391 Scalvini B. et al., Circuit Topology Approach for the Comparative Analysis of Intrinsically Disordered Proteins. J. Chem. Inf. Model. 63, 8, 2586–2602 (2023)]&lt;/ref&gt; By employing a topological approach, one can categorize motifs according to their topological buildup and the timescale of their formation.</div></td></tr> <tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr> <tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>A common aspect of IDP structural ensembles is the ability or tendency to fold upon an interaction to a binding partner in the cell. Examples of IDP folding in a binding context are binding-coupled folding,&lt;ref&gt;{{Cite journal |last=Robustelli |first=Paul |last2=Piana |first2=Stefano |last3=Shaw |first3=David E. |date=2020-04-23 |title=Mechanism of Coupled Folding-upon-Binding of an Intrinsically Disordered Protein |url=https://doi.org/10.1021/jacs.0c03217 |journal=Journal of the American Chemical Society |volume=142 |issue=25 |pages=11092–11101 |doi=10.1021/jacs.0c03217 |issn=0002-7863}}&lt;/ref&gt; and formation of fuzzy complexes.&lt;ref&gt;{{Cite journal |last=Tompa |first=Peter |last2=Fuxreiter |first2=Monika |date=January 2008 |title=Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions |url=https://doi.org/10.1016/j.tibs.2007.10.003 |journal=Trends in Biochemical Sciences |volume=33 |issue=1 |pages=2–8 |doi=10.1016/j.tibs.2007.10.003 |issn=0968-0004|url-access=subscription }}&lt;/ref&gt; However, it is also possible for proteins to remain entirely disordered in a binding scenario.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>A common aspect of IDP structural ensembles is the ability or tendency to fold upon an interaction to a binding partner in the cell. Examples of IDP folding in a binding context are binding-coupled folding,&lt;ref&gt;{{Cite journal |last=Robustelli |first=Paul |last2=Piana |first2=Stefano |last3=Shaw |first3=David E. |date=2020-04-23 |title=Mechanism of Coupled Folding-upon-Binding of an Intrinsically Disordered Protein |url=https://doi.org/10.1021/jacs.0c03217 |journal=Journal of the American Chemical Society |volume=142 |issue=25 |pages=11092–11101 |doi=10.1021/jacs.0c03217 |issn=0002-7863<ins style="font-weight: bold; text-decoration: none;">|url-access=subscription </ins>}}&lt;/ref&gt; and formation of fuzzy complexes.&lt;ref&gt;{{Cite journal |last=Tompa |first=Peter |last2=Fuxreiter |first2=Monika |date=January 2008 |title=Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions |url=https://doi.org/10.1016/j.tibs.2007.10.003 |journal=Trends in Biochemical Sciences |volume=33 |issue=1 |pages=2–8 |doi=10.1016/j.tibs.2007.10.003 |issn=0968-0004|url-access=subscription }}&lt;/ref&gt; However, it is also possible for proteins to remain entirely disordered in a binding scenario.</div></td></tr> <tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr> <tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Experimental validation==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Experimental validation==</div></td></tr> </table>

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