Ontology highlight
ABSTRACT:
SUBMITTER: Walti MA
PROVIDER: S-EPMC6029692 | biostudies-literature | 2018 Jun
REPOSITORIES: biostudies-literature
Wälti Marielle A MA Libich David S DS Clore G Marius GM
The journal of physical chemistry letters 20180607 12
The chaperonin GroEL is a 800 kDa nanomachine comprising two heptameric rings, each of which encloses a large cavity or folding chamber. The GroEL cycle involves ATP-dependent capping of the cavity by the cochaperone GroES to create a nanocage in which a single protein molecule can fold. We investigate how protein substrates sample the cavity prior to encapsulation by GroES using paramagnetic relaxation enhancement to detect transient, sparsely populated interactions between apo GroEL, paramagne ...[more]