Ontology highlight
ABSTRACT:
SUBMITTER: Sikor M
PROVIDER: S-EPMC3671257 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature
The EMBO journal 20130426 11
The numerous functions of the important class of molecular chaperones, heat shock proteins 70 (Hsp70), rely on cycles of intricate conformational changes driven by ATP-hydrolysis and regulated by cochaperones and substrates. Here, we used Förster resonance energy transfer to study the conformational dynamics of individual molecules of Ssc1, a mitochondrial Hsp70, in real time. The intrinsic dynamics of the substrate-binding domain of Ssc1 was observed to be uncoupled from the dynamic interaction ...[more]