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A Role for Confined Water in Chaperonin Function

Overview
Journal J Am Chem Soc
Publisher American Chemical Society
Specialty Chemistry
Date 2008 Aug 20
PMID 18710231
Citations 23
Authors
Jeremy L England
Del Lucent
Vijay S Pande
Affiliations
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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.

Citing Articles

A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.

Korobko I, Eberle R, Roy M, Horovitz A Proc Natl Acad Sci U S A. 2022; 119(48):e2213170119.

PMID: 36409898 PMC: 9860310. DOI: 10.1073/pnas.2213170119.

Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones.

Xu H Biomolecules. 2022; 12(6).

PMID: 35740957 PMC: 9221429. DOI: 10.3390/biom12060832.

Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes.

Sadat A, Tiwari S, Sunidhi S, Chaphalkar A, Kochar M, Ali M Proc Natl Acad Sci U S A. 2022; 119(18):e2118465119.

PMID: 35486698 PMC: 9170145. DOI: 10.1073/pnas.2118465119.

Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity.

Macro N, Chen L, Yang Y, Mondal T, Wang L, Horovitz A J Phys Chem Lett. 2021; 12(24):5723-5730.

PMID: 34129341 PMC: 8687601. DOI: 10.1021/acs.jpclett.1c01216.

Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.

Korobko I, Mazal H, Haran G, Horovitz A Elife. 2020; 9.

PMID: 32716842 PMC: 7440923. DOI: 10.7554/eLife.56511.

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