Article

Local unfolding of the HSP27 monomer regulates chaperone activity

2018-06-14

Abstract excerpt

The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the human body. Here we describe redox-induced changes to the structure, dynamics, and function of HSP27 and its conserved α-crystallin domain, and provide the first structural characterization of a small heat-shock protein monomer. While HSP27 assembles into oligomers, we show that the transiently populated mo...

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Literature Corpus work: 43bc338e-a7a1-579e-b818-5c092e416771
DOI: 10.1101/345751

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