Efficient conversion of chemical energy into mechanical work by Hsp70 chaperones

• DOI: 10.48550/arxiv.1902.01612
• Publication Date: 2019-01-01
• Authors: Salvatore Assenza; Alberto Stefano S...; Ruth Kellner; Benjamin Schuler; Paolo De Los Rios; Alessandro Barducci
• Keywords: Chaperone (clinical)

Hsp70 molecular chaperones are abundant ATP-dependent nanomachines that actively reshape non-native, misfolded proteins and assist a wide variety of essential cellular processes. Here we combine complementary computational/theoretical approaches to elucidate the structural thermodynamic details chaperone-induced expansion substrate protein, with particular emphasis on critical role played by ATP hydrolysis. We first determine conformational free-energy cost due binding multiple using coarse-grained simulations. then exploit this result implement non-equilibrium rate model which estimates degree as function free energy provided Our results in quantitative agreement recent single-molecule FRET experiments highlight stark nature process, showing Hsp70s optimized convert effectively chemical into mechanical work close physiological conditions.