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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Autores principales: Mingchen Chen, Xun Chen, Nicholas P. Schafer, Cecilia Clementi, Elizabeth A. Komives, Diego U. Ferreiro, Peter G. Wolynes
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://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
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