Protein tertiary structure recognition using optimized Hamiltonians with local interactions

Richard A. Goldstein; Zaida A. Luthey-Schulten; Peter G. Wolynes

doi:10.1073/pnas.89.19.9029

Protein tertiary structure recognition using optimized Hamiltonians with local interactions

Richard A. Goldstein, Zaida A. Luthey-Schulten, Peter G. Wolynes

Research output: Contribution to journal › Article › peer-review

Abstract

Protein folding codes embodying local interactions including surface and secondary structure propensities and residue-residue contacts are optimized for a set of training proteins by using spin-glass theory. A screening method based on these codes correctly matches the structure of a set of test proteins with proteins of similar topology with 100% accuracy, even with limited sequence similarity between the test proteins and the structural homologs and the absence of any structurally similar proteins in the training set.

Original language	English (US)
Pages (from-to)	9029-9033
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	89
Issue number	19
DOIs	https://doi.org/10.1073/pnas.89.19.9029
State	Published - Oct 1 1992

Keywords

Protein structure prediction
Spin-glass theory

ASJC Scopus subject areas

General

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10.1073/pnas.89.19.9029

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AU - Luthey-Schulten, Zaida A.

AU - Wolynes, Peter G.

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AB - Protein folding codes embodying local interactions including surface and secondary structure propensities and residue-residue contacts are optimized for a set of training proteins by using spin-glass theory. A screening method based on these codes correctly matches the structure of a set of test proteins with proteins of similar topology with 100% accuracy, even with limited sequence similarity between the test proteins and the structural homologs and the absence of any structurally similar proteins in the training set.

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Protein tertiary structure recognition using optimized Hamiltonians with local interactions

Abstract

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