Ontology highlight
ABSTRACT:
SUBMITTER: Dalton KM
PROVIDER: S-EPMC4379175 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Dalton Kevin M KM Frydman Judith J Pande Vijay S VS
PloS one 20150330 3
Chaperonins are large ring shaped oligomers that facilitate protein folding by encapsulation within a central cavity. All chaperonins possess flexible C-termini which protrude from the equatorial domain of each subunit into the central cavity. Biochemical evidence suggests that the termini play an important role in the allosteric regulation of the ATPase cycle, in substrate folding and in complex assembly and stability. Despite the tremendous wealth of structural data available for numerous orth ...[more]