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PMID: 7724609 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Toward an outline of the topography of a realistic protein-folding funnel.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 92 ·No. 8 ·1995-04-11 ·Pages 3626-30

Onuchic JN, Wolynes PG, Luthey-Schulten Z, Socci ND

Abstract

Experimental information on the structure and dynamics of molten globules gives estimates for the energy landscape's characteristics for folding highly helical proteins, when supplemented by a theory of the helix-coil transition in collapsed heteropolymers. A law of corresponding states relating simulations on small lattice models to real proteins possessing many more degrees of freedom results. This correspondence reveals parallels between "minimalist" lattice results and recent experimental results for the degree of native character of the folding transition state and molten globule and also pinpoints the needs of further experiments.

MeSH Terms
Computer Simulation Models, Chemical Protein Conformation Protein Folding
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Onuchic J N
School of Chemical Sciences, University of Illinois, Urbana 61801, USA.
Wolynes P G
Luthey-Schulten Z
Socci N D
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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.92.8.3626
Published
1995-04-11
Pages
3626-30
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC42220
Subset
IM
Grants
NIGMS NIH HHS · 1R01 GM44557 · United States
External Links
PubMed source DOI: 10.1073/pnas.92.8.3626 PMC Full Text View journal details
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