Prying open single GroES ring complexes by force reveals cooperativity across domains.

ABSTRACT: Understanding how the mechanical properties of a protein complex emerge from the interplay of intra- and interchain interactions is vital at both fundamental and applied levels. To investigate whether interdomain cooperativity affects protein mechanical strength, we employed single-molecule force spectroscopy to probe the mechanical stability of GroES, a homoheptamer with a domelike quaternary stucture stabilized by intersubunit interactions between the first and last β-strands of adjacent domains. A GroES variant was constructed in which each subunit of the GroES heptamer is covalently linked to adjacent subunits by tripeptide linkers and folded domains of protein L are introduced to the heptamer's termini as handle molecules. The force-distance profiles for GroES unfolding showed, for th

SUBMITTER: Ikeda-Kobayashi A 

PROVIDER: S-EPMC3328714 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature