Surveying biomolecular frustration at atomic resolution

The analysis of biomolecular frustration yielded insights into several aspects of protein behavior. Here the authors describe a framework to efficiently quantify and localize biomolecular frustration within proteins at atomic resolution, and observe that drug specificity is correlated with a minimal...

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Main Authors:	Mingchen Chen, Xun Chen, Nicholas P. Schafer, Cecilia Clementi, Elizabeth A. Komives, Diego U. Ferreiro, Peter G. Wolynes
Format:	article
Language:	EN
Published:	Nature Portfolio 2020
Subjects:	Science Q
Online Access:	https://doaj.org/article/faf469d2c6054cd7b15e2d03d0f96484
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id	oai:doaj.org-article:faf469d2c6054cd7b15e2d03d0f96484
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spelling	oai:doaj.org-article:faf469d2c6054cd7b15e2d03d0f964842021-12-02T10:48:29ZSurveying biomolecular frustration at atomic resolution10.1038/s41467-020-19560-92041-1723https://doaj.org/article/faf469d2c6054cd7b15e2d03d0f964842020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19560-9https://doaj.org/toc/2041-1723The analysis of biomolecular frustration yielded insights into several aspects of protein behavior. Here the authors describe a framework to efficiently quantify and localize biomolecular frustration within proteins at atomic resolution, and observe that drug specificity is correlated with a minimally frustrated binding pocket leading to a funneled binding landscape.Mingchen ChenXun ChenNicholas P. SchaferCecilia ClementiElizabeth A. KomivesDiego U. FerreiroPeter G. WolynesNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Mingchen Chen Xun Chen Nicholas P. Schafer Cecilia Clementi Elizabeth A. Komives Diego U. Ferreiro Peter G. Wolynes Surveying biomolecular frustration at atomic resolution
description	The analysis of biomolecular frustration yielded insights into several aspects of protein behavior. Here the authors describe a framework to efficiently quantify and localize biomolecular frustration within proteins at atomic resolution, and observe that drug specificity is correlated with a minimally frustrated binding pocket leading to a funneled binding landscape.
format	article
author	Mingchen Chen Xun Chen Nicholas P. Schafer Cecilia Clementi Elizabeth A. Komives Diego U. Ferreiro Peter G. Wolynes
author_facet	Mingchen Chen Xun Chen Nicholas P. Schafer Cecilia Clementi Elizabeth A. Komives Diego U. Ferreiro Peter G. Wolynes
author_sort	Mingchen Chen
title	Surveying biomolecular frustration at atomic resolution
title_short	Surveying biomolecular frustration at atomic resolution
title_full	Surveying biomolecular frustration at atomic resolution
title_fullStr	Surveying biomolecular frustration at atomic resolution
title_full_unstemmed	Surveying biomolecular frustration at atomic resolution
title_sort	surveying biomolecular frustration at atomic resolution
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/faf469d2c6054cd7b15e2d03d0f96484
work_keys_str_mv	AT mingchenchen surveyingbiomolecularfrustrationatatomicresolution AT xunchen surveyingbiomolecularfrustrationatatomicresolution AT nicholaspschafer surveyingbiomolecularfrustrationatatomicresolution AT ceciliaclementi surveyingbiomolecularfrustrationatatomicresolution AT elizabethakomives surveyingbiomolecularfrustrationatatomicresolution AT diegouferreiro surveyingbiomolecularfrustrationatatomicresolution AT petergwolynes surveyingbiomolecularfrustrationatatomicresolution
_version_	1718396686610464768

Surveying biomolecular frustration at atomic resolution

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