A role for confined water in chaperonin function.

ABSTRACT: Chaperonins engulf other proteins and accelerate their folding by an unknown mechanism. Here, we combine all-atom molecular dynamics simulations with data from experimental assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin's ability to facilitate folding is correlated with the affinity of its interior surface for water. Our results suggest a novel view of the behavior of confined water for models of in vivo protein folding scenarios.

SUBMITTER: England JL 

PROVIDER: S-EPMC2646679 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature