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Protein tertiary structure recognition using optimized Hamiltonians with local interactions.


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.

SUBMITTER: Goldstein RA 

PROVIDER: S-EPMC50058 | biostudies-other | 1992 Oct

REPOSITORIES: biostudies-other

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Protein tertiary structure recognition using optimized Hamiltonians with local interactions.

Goldstein R A RA   Luthey-Schulten Z A ZA   Wolynes P G PG  

Proceedings of the National Academy of Sciences of the United States of America 19921001 19


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 prot  ...[more]

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