Non-equilibrium conformational dynamics in the function of molecular chaperones

Alessandro Barducci; Paolo De Los Rios

doi:10.1016/j.sbi.2015.02.008

Non-equilibrium conformational dynamics in the function of molecular chaperones

Curr Opin Struct Biol. 2015 Feb:30:161-169. doi: 10.1016/j.sbi.2015.02.008. Epub 2015 Mar 13.

Authors

Alessandro Barducci¹, Paolo De Los Rios²

Affiliations

¹ Laboratoire de Biophysique Statistique, School of Basic Sciences, École Polytechnique Fédérale de Lausanne (EPFL), CH 1015 Lausanne, Switzerland. Electronic address: alessandro.barducci@epfl.ch.
² Laboratoire de Biophysique Statistique, School of Basic Sciences, École Polytechnique Fédérale de Lausanne (EPFL), CH 1015 Lausanne, Switzerland. Electronic address: paolo.delosrios@epfl.ch.

PMID: 25771489
DOI: 10.1016/j.sbi.2015.02.008

Abstract

Why do chaperones need ATP hydrolysis to help proteins reach their native, functional states? In this review, we highlight the most recent experimental and theoretical evidences suggesting that ATP hydrolysis allows molecular chaperones to escape the bounds imposed by equilibrium thermodynamics. We argue here that energy consumption must be fully taken into account to understand the mechanism of these intrinsically non-equilibrium machines and we propose a novel perspective in the way the relation between function and ATP hydrolysis is viewed.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adenosine Triphosphatases / metabolism*
Energy Metabolism / physiology*
Heat-Shock Proteins / metabolism*
Hydrolysis
Models, Biological*
Models, Molecular*
Molecular Chaperones / chemistry*
Molecular Chaperones / metabolism
Protein Conformation*
Protein Structure, Tertiary
Thermodynamics

Substances

Heat-Shock Proteins
Molecular Chaperones
Adenosine Triphosphatases