Protein tertiary structure recognition using optimized Hamiltonians with local interactions.

R A Goldstein; Z A Luthey-Schulten; P G Wolynes

doi:10.1073/pnas.89.19.9029

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Protein tertiary structure recognition using optimized Hamiltonians with local interactions.

R A Goldstein·Z A Luthey-Schulten·P G Wolynes

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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.

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Amino Acids Animals Humans Mathematics Models, Theoretical Protein Folding Protein Structure, Tertiary Journal Article Research Support, U.S. Gov't, P.H.S.

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R A Goldstein, Z A Luthey-Schulten, P G Wolynes. 1992-10-01. Protein tertiary structure recognition using optimized Hamiltonians with local interactions.. https://doi.org/10.1073/pnas.89.19.9029

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