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A Role for Confined Water in Chaperonin Function
[Image: see text] Chaperonins engulf other proteins and accelerate their folding by an unknown mechanism. Here, we combine all-atom molecular dynamics simulations with data from experimental assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin’s ability to facili...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2646679/ https://www.ncbi.nlm.nih.gov/pubmed/18710231 http://dx.doi.org/10.1021/ja802248m |
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author | England, Jeremy L. Lucent, Del Pande, Vijay S. |
author_facet | England, Jeremy L. Lucent, Del Pande, Vijay S. |
author_sort | England, Jeremy L. |
collection | PubMed |
description | [Image: see text] Chaperonins engulf other proteins and accelerate their folding by an unknown mechanism. Here, we combine all-atom molecular dynamics simulations with data from experimental assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin’s ability to facilitate folding is correlated with the affinity of its interior surface for water. Our results suggest a novel view of the behavior of confined water for models of in vivo protein folding scenarios. |
format | Text |
id | pubmed-2646679 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-26466792009-03-20 A Role for Confined Water in Chaperonin Function England, Jeremy L. Lucent, Del Pande, Vijay S. J Am Chem Soc [Image: see text] Chaperonins engulf other proteins and accelerate their folding by an unknown mechanism. Here, we combine all-atom molecular dynamics simulations with data from experimental assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin’s ability to facilitate folding is correlated with the affinity of its interior surface for water. Our results suggest a novel view of the behavior of confined water for models of in vivo protein folding scenarios. American Chemical Society 2008-08-19 2008-09-10 /pmc/articles/PMC2646679/ /pubmed/18710231 http://dx.doi.org/10.1021/ja802248m Text en Copyright © 2008 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org. 40.75 |
spellingShingle | England, Jeremy L. Lucent, Del Pande, Vijay S. A Role for Confined Water in Chaperonin Function |
title | A Role for Confined Water in Chaperonin Function |
title_full | A Role for Confined Water in Chaperonin Function |
title_fullStr | A Role for Confined Water in Chaperonin Function |
title_full_unstemmed | A Role for Confined Water in Chaperonin Function |
title_short | A Role for Confined Water in Chaperonin Function |
title_sort | role for confined water in chaperonin function |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2646679/ https://www.ncbi.nlm.nih.gov/pubmed/18710231 http://dx.doi.org/10.1021/ja802248m |
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