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Predicting the energetics of osmolyte-induced protein folding/unfolding.

ABSTRACT: A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved. Moreover, the approach permits dissection of the folding/unfolding free-energy changes into individual contributions from the peptide backbone and residue side chains.

SUBMITTER: Auton M

PROVIDER: S-EPMC1257718 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature

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Predicting the energetics of osmolyte-induced protein folding/unfolding.

Auton Matthew M Bolen D Wayne DW

Proceedings of the National Academy of Sciences of the United States of America 20051007 42

A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved. Moreover, the approach permits di ...[more]

PMID: 16214887

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