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PMID: 9023333 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structural correlations in protein folding funnels.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 94 ·No. 3 ·1997-02-04 ·Pages 777-82

Shoemaker BA, Wang J, Wolynes PG

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.

MeSH Terms
Amino Acids/chemistry Entropy Peptides/chemistry Plant Proteins Protein Denaturation Protein Folding Protein Structure, Tertiary
Chemicals
Amino Acids Peptides Plant Proteins chymotrypsin inhibitor 2
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Shoemaker B A
School of Chemical Sciences, University of Illinois, Urbana 61801, USA.
Wang J
Wolynes P G
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.94.3.777
Published
1997-02-04
Pages
777-82
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC19590
Subset
IM
Grants
NIGMS NIH HHS · R01 GM044557 · United States
NIGMS NIH HHS · R01 GM44557 · United States
External Links
PubMed source DOI: 10.1073/pnas.94.3.777 PMC Full Text View journal details
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