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The mechanism of Hsp70 chaperones: (entropic) pulling the models together.
Trends in Biochemical Sciences
Hsp70s are conserved molecular chaperones that can prevent protein aggregation, actively unfold, solubilize aggregates, pull translocating proteins across membranes and remodel native proteins complexes. Disparate mechanisms have been proposed for the various modes of Hsp70 action: passive prevention of aggregation by kinetic partitioning, peptide-bond isomerase, Brownian ratcheting or active power-stroke pulling. Recently, we put forward a unifying mechanism named 'entropic pulling', which proposed that Hsp70 uses the energy of ATP hydrolysis to recruit a force of entropic origin to locally unfold aggregates or pull proteins across membranes. The entropic pulling mechanism reproduces the expected phenomenology that inspired the other disparate mechanisms and is, moreover, simple.
Adenosine Triphosphate/chemistry, Animals, Binding Sites, Entropy, HSP70 Heat-Shock Proteins/physiology, Humans, Hydrolysis, Kinetics, Models, Molecular, Molecular Chaperones/chemistry, Molecular Chaperones/metabolism, Molecular Conformation, Peptides/chemistry, Protein Conformation, Protein Denaturation, Protein Folding
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