Energy landscape remodeling mechanism of Hsp70-chaperone-accelerated protein folding.

ABSTRACT: Hsp70 chaperone is one of the key protein machines responsible for the quality control of protein production in cells. Facilitating in vivo protein folding by counteracting misfolding and aggregation is the essence of its biological function. Although the allosteric cycle during its functional actions has been well characterized both experimentally and computationally, the mechanism by which Hsp70 assists protein folding is still not fully understood. In this work, we studied the Hsp70-mediated folding of model proteins with rugged energy landscape by using molecular simulations. Different from the canonical scenario of Hsp70 functioning, which assumes that folding of substrate proteins occurs spontaneously after releasing from chaperones, our results showed that the substrate protein rema

SUBMITTER: Lu J 

PROVIDER: S-EPMC8204389 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature