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Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):777-82.

Structural correlations in protein folding funnels.

Author information

1
School of Chemical Sciences, University of Illinois, Urbana 61801, USA.

Abstract

While the overall energy landscape of a foldable protein can be described by means of a few parameters characterizing its statistical topography, specific energetic terms subtly bias the representative structures giving rise to residue pair correlations as in a liquid. We use a free energy functional incorporating an inhomogeneous pair contact energy along with a contact formation entropy and a cooperativity contribution to determine residue-specific contact probabilities in the denatured state and the transition state ensemble. The predicted "hot residues" for the theoretical transition state ensemble reasonably agree with experiment for chymotrypsin inhibitor 2, and generally a strong correlation exists with the measured kinetic effects of mutating residues not involved in highly solvent-exposed regions.

PMID:
9023333
PMCID:
PMC19590
[Indexed for MEDLINE]
Free PMC Article

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