title: Non-equilibrium conformational dynamics in the function of molecular chaperones.
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.
authors.affiliation: Laboratoire de Biophysique Statistique, School of Basic Sciences, École Polytechnique Fédérale de Lausanne (EPFL), CH 1015 Lausanne, Switzerland. Electronic address: alessandro.barducci@epfl.ch.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Barducci
authors.affiliation: Laboratoire de Biophysique Statistique, School of Basic Sciences, École Polytechnique Fédérale de Lausanne (EPFL), CH 1015 Lausanne, Switzerland. Electronic address: paolo.delosrios@epfl.ch.
authors.forename: Paolo
authors.initials: P
authors.lastname: De Los Rios
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D004734:Energy Metabolism / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006868:Hydrolysis; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
chemical_list: D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D000251:Adenosine Triphosphatases