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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4489264/ https://www.ncbi.nlm.nih.gov/pubmed/25883149 http://dx.doi.org/10.1093/nar/gkv343 |
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author | Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J. |
author_facet | Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J. |
author_sort | Frappier, Vincent |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-4489264 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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. Nucleic Acids Res 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. |
spellingShingle | Web Server issue Frappier, Vincent Chartier, Matthieu Najmanovich, Rafael J. ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability |
title | 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_short | 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 |
topic | Web Server issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4489264/ https://www.ncbi.nlm.nih.gov/pubmed/25883149 http://dx.doi.org/10.1093/nar/gkv343 |
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