ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability

ENCoM is a coarse-grained normal mode analysis method recently introduced that unlike previous such methods is unique in that it accounts for the nature of amino acids. The inclusion of this layer of information was shown to improve conformational space sampling and apply for the first time a coarse...

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Main Authors:	Frappier, Vincent, Chartier, Matthieu, Najmanovich, Rafael J.
Format:	Online
Language:	English
Published:	Oxford University Press 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4489264/

id	pubmed-4489264
recordtype	oai_dc
spelling	pubmed-44892642015-07-07 ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J. Web Server issue ENCoM is a coarse-grained normal mode analysis method recently introduced that unlike previous such methods is unique in that it accounts for the nature of amino acids. The inclusion of this layer of information was shown to improve conformational space sampling and apply for the first time a coarse-grained normal mode analysis method to predict the effect of single point mutations on protein dynamics and thermostability resulting from vibrational entropy changes. Here we present a web server that allows non-technical users to have access to ENCoM calculations to predict the effect of mutations on thermostability and dynamics as well as to generate geometrically realistic conformational ensembles. The server is accessible at: http://bcb.med.usherbrooke.ca/encom. Oxford University Press 2015-07-01 2015-04-16 /pmc/articles/PMC4489264/ /pubmed/25883149 http://dx.doi.org/10.1093/nar/gkv343 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J.
spellingShingle	Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J. ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
author_facet	Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J.
author_sort	Frappier, Vincent
title	ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
title_short	ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
title_full	ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
title_fullStr	ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
title_full_unstemmed	ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
title_sort	encom server: exploring protein conformational space and the effect of mutations on protein function and stability
description	ENCoM is a coarse-grained normal mode analysis method recently introduced that unlike previous such methods is unique in that it accounts for the nature of amino acids. The inclusion of this layer of information was shown to improve conformational space sampling and apply for the first time a coarse-grained normal mode analysis method to predict the effect of single point mutations on protein dynamics and thermostability resulting from vibrational entropy changes. Here we present a web server that allows non-technical users to have access to ENCoM calculations to predict the effect of mutations on thermostability and dynamics as well as to generate geometrically realistic conformational ensembles. The server is accessible at: http://bcb.med.usherbrooke.ca/encom.
publisher	Oxford University Press
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4489264/
_version_	1613243103004590080

ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability

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