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	<title>2020Abriata Review - Revision history</title>
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	<updated>2026-05-24T21:06:42Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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	<entry>
		<id>https://3demmethods.i2pc.es/index.php?title=2020Abriata_Review&amp;diff=3773&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Abriata, L. A.; Dal Peraro, M. Will Cryo-Electron Microscopy Shift the Current Paradigm in Protein Structure Prediction? Journal of chemical information and mo...&quot;</title>
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		<updated>2020-07-30T07:33:41Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Abriata, L. A.; Dal Peraro, M. Will Cryo-Electron Microscopy Shift the Current Paradigm in Protein Structure Prediction? Journal of chemical information and mo...&amp;quot;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;== Citation ==&lt;br /&gt;
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Abriata, L. A.; Dal Peraro, M. Will Cryo-Electron Microscopy Shift the Current Paradigm in Protein Structure Prediction? Journal of chemical information and modeling, 2020, 60, 2443-2447 &lt;br /&gt;
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== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Protein dynamics is undoubtedly a pervasive ingredient in all biological functions. However, structural biology has been strongly driven by a static-centered view of protein architecture. We argue that the recent advances of cryo-electron microscopy (EM) have the potential to more broadly explore the conformational landscapes of protein complexes and therefore will enhance our ability to predict the diverse conformations of tertiary and quaternary protein structures that are functionally relevant in physiological conditions. &lt;br /&gt;
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== Keywords ==&lt;br /&gt;
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== Links ==&lt;br /&gt;
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https://pubs.acs.org/doi/10.1021/acs.jcim.0c00177&lt;br /&gt;
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== Related software ==&lt;br /&gt;
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== Related methods ==&lt;br /&gt;
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== Comments ==&lt;/div&gt;</summary>
		<author><name>WikiSysop</name></author>
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