Protein tertiary structure recognition using optimized Hamiltonians with local interactions.

Goldstein, R A; Luthey-Schulten, Z A; Wolynes, P G · Proc Natl Acad Sci U S A · 1992

basic_science · Level V

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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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