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J Am Chem Soc. 2008 Sep 10;130(36):11838-9. doi: 10.1021/ja802248m. Epub 2008 Aug 19.

A role for confined water in chaperonin function.

Author information

1
James H. Clark Center, S297, Stanford University, Stanford, California 94305, USA.

Abstract

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.

PMID:
18710231
PMCID:
PMC2646679
DOI:
10.1021/ja802248m
[Indexed for MEDLINE]
Free PMC Article
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