Mechanisms and kinetics of beta-hairpin formation.

ABSTRACT: Thermodynamics and kinetics of off-lattice models with side chains for the beta-hairpin fragment of immunoglobulin-binding protein and its variants are reported. For all properties (except refolding time tau(F)) there are no qualitative differences between the full model and the Go version. The validity of the models is established by comparison of the calculated native structure with the Protein Data Bank coordinates and by reproducing the experimental results for the degree of cooperativity and tau(F). For the full model tau(F) approximately 2 micros at the folding temperature (experimental value is 6 micros); the Go model folds 50 times faster. Upon refolding, structural changes take place over three time scales. On the collapse time scale compact structures with intact hydrophobic clus

SUBMITTER: Klimov DK 

PROVIDER: S-EPMC15965 | biostudies-literature | 2000 Mar

REPOSITORIES: biostudies-literature