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

ABSTRACT: Recent experimental studies suggest that ATP-driven molecular chaperones can stabilize protein substrates in their native structures out of thermal equilibrium. The mechanism of such non-equilibrium protein folding is an open question. Based on available structural and biochemical evidence, I propose here a unifying principle that underlies the conversion of chemical energy from ATP hydrolysis to the conformational free energy associated with protein folding and activation. I demonstrate that non-equilibrium folding requires the chaperones to break at least one of four symmetry conditions. The Hsp70 and Hsp90 chaperones each break a different subset of these symmetries and thus they use different mechanisms for non-equilibrium protein folding. I derive an upper bound on the non-equilibrium

SUBMITTER: Xu H 

PROVIDER: S-EPMC9221429 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature