Ontology highlight
ABSTRACT:
SUBMITTER: Wu K
PROVIDER: S-EPMC6811625 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Wu Kevin K Stull Frederick F Lee Changhan C Bardwell James C A JCA
Nature communications 20191023 1
It is generally assumed that protein clients fold following their release from chaperones instead of folding while remaining chaperone-bound, in part because binding is assumed to constrain the mobility of bound clients. Previously, we made the surprising observation that the ATP-independent chaperone Spy allows its client protein Im7 to fold into the native state while continuously bound to the chaperone. Spy apparently permits sufficient client mobility to allow folding to occur while chaperon ...[more]