Ontology highlight
ABSTRACT:
SUBMITTER: Sato S
PROVIDER: S-EPMC406447 | biostudies-literature | 2004 May
REPOSITORIES: biostudies-literature
Sato Satoshi S Religa Tomasz L TL Daggett Valerie V Fersht Alan R AR
Proceedings of the National Academy of Sciences of the United States of America 20040406 18
We have assessed the published predictions of the pathway of folding of the B domain of protein A, the pathway most studied by computer simulation. We analyzed the transition state for folding of the three-helix bundle protein, by using experimental Phi values on some 70 suitable mutants. Surprisingly, the third helix, which has the most stable alpha-helical structure as a peptide fragment, is poorly formed in the transition state, especially at its C terminus. The protein folds around a nearly ...[more]