Ontology highlight
ABSTRACT:
SUBMITTER: Hyeon C
PROVIDER: S-EPMC1748156 | biostudies-literature | 2006 Dec
REPOSITORIES: biostudies-literature
Hyeon Changbong C Lorimer George H GH Thirumalai D D
Proceedings of the National Academy of Sciences of the United States of America 20061129 50
The chaperonin GroEL-GroES, a machine that helps proteins to fold, cycles through a number of allosteric states, the T state, with high affinity for substrate proteins, the ATP-bound R state, and the R" (GroEL-ADP-GroES) complex. Here, we use a self-organized polymer model for the GroEL allosteric states and a general structure-based technique to simulate the dynamics of allosteric transitions in two subunits of GroEL and the heptamer. The T --> R transition, in which the apical domains undergo ...[more]