Ontology highlight
ABSTRACT:
SUBMITTER: Alderson TR
PROVIDER: S-EPMC6403371 | biostudies-literature | 2019 Mar
REPOSITORIES: biostudies-literature
Nature communications 20190306 1
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 (ACD). While HSP27 assembles into oligomers, we show that the monomers formed upon reduction are highly active chaperones in vitro, but are susceptible to self-aggregation. By using relaxation dispersion and high-pressure nuclear magnetic resonance (N ...[more]