Ontology highlight
ABSTRACT:
SUBMITTER: England JL
PROVIDER: S-EPMC2646679 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
England Jeremy L JL Lucent Del D Pande Vijay S VS
Journal of the American Chemical Society 20080819 36
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. ...[more]