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PMID: 1594594 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Optimal protein-folding codes from spin-glass theory.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 11 ·1992-06-01 ·Pages 4918-22

Goldstein RA, Luthey-Schulten ZA, Wolynes PG

Abstract

Protein-folding codes embodied in sequence-dependent energy functions can be optimized using spin-glass theory. Optimal folding codes for associative-memory Hamiltonians based on aligned sequences are deduced. A screening method based on these codes correctly recognizes protein structures in the "twilight zone" of sequence identity in the overwhelming majority of cases. Simulated annealing for the optimally encoded Hamiltonian generally leads to qualitatively correct structures.

MeSH Terms

Bence Jones Protein/ultrastructure Crystallography DNA-Binding Proteins Humans In Vitro Techniques Models, Molecular Models, Theoretical Protein Conformation Repressor Proteins/ultrastructure Solubility Thermodynamics Viral Proteins Viral Regulatory and Accessory Proteins Water

Chemicals

DNA-Binding Proteins Repressor Proteins Viral Proteins Viral Regulatory and Accessory Proteins phage repressor proteins Water Bence Jones Protein

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Goldstein R A

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

Luthey-Schulten Z A

Wolynes P G

References (12)

12 references, click to expand

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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.89.11.4918

Published

1992-06-01

Pages

4918-22

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC49199

Subset

Grants

NIGMS NIH HHS · GM44557-01 · United States

External Links

PubMed source DOI: 10.1073/pnas.89.11.4918 PMC Full Text View journal details

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