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. 1992 Oct 1;89(19):9029–9033. doi: 10.1073/pnas.89.19.9029

Protein tertiary structure recognition using optimized Hamiltonians with local interactions.

R A Goldstein 1, Z A Luthey-Schulten 1, P G Wolynes 1
PMCID: PMC50058  PMID: 1409599

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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Selected References

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