Non-equilibrium conformational dynamics in the function of molecular chaperones

Current Opinion in Structural Biology
Alessandro Barducci, Paolo De Los Rios

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.

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Citations

Dec 9, 2017·Proceedings of the National Academy of Sciences of the United States of America·Shaon ChakrabartiD Thirumalai
Mar 7, 2018·Nature Chemical Biology·Pierre GoloubinoffPaolo De Los Rios
Dec 18, 2019·ELife·Salvatore AssenzaAlessandro Barducci
Apr 23, 2020·Journal of the Royal Society, Interface·Pencho Yordanov, Jörg Stelling
May 14, 2020·International Journal of Molecular Sciences·Malgorzata KleczewskaRafal Dutkiewicz
Nov 3, 2020·Journal of Biomolecular NMR·Sebastian Hiller
Feb 27, 2021·F1000Research·Harutyun SahakyanIrina Sorokina

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