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Variations in the fast folding rates of the lambda-repressor: a hybrid molecular dynamics study.

ABSTRACT: The ability to predict the effects of mutations on protein folding rates and mechanisms would greatly facilitate folding studies. Using a realistic full atom potential coupled with a G?-like potential biased to the native state structure, we have investigated the effects of point mutations on the folding rates of a small single domain protein. The hybrid potential provides a detailed level of description of the folding mechanism that we correlate to features of the folding energy landscapes of fast and slow mutants of an 80-residue-long fragment of the lambda-repressor. Our computational reconstruction of the folding events is compared to the recent experimental results of W. Y. Yang and M. Gruebele (see companion article) and T. G. Oas and co-workers on the lambda-repressor, and helps to clarify the differences observed in the folding mechanisms of the various mutants.

SUBMITTER: Pogorelov TV

PROVIDER: S-EPMC1304343 | biostudies-literature | 2004 Jul

REPOSITORIES: biostudies-literature

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Variations in the fast folding rates of the lambda-repressor: a hybrid molecular dynamics study.

Pogorelov Taras V TV Luthey-Schulten Zaida Z

Biophysical journal 20040701 1

The ability to predict the effects of mutations on protein folding rates and mechanisms would greatly facilitate folding studies. Using a realistic full atom potential coupled with a Gō-like potential biased to the native state structure, we have investigated the effects of point mutations on the folding rates of a small single domain protein. The hybrid potential provides a detailed level of description of the folding mechanism that we correlate to features of the folding energy landscapes of f ...[more]

PMID: 15240458

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