Protein tertiary structure recognition using optimized Hamiltonians with local interactions.
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.
Goldstein
R A
RA
School of Chemical Sciences, University of Illinois, Urbana 61801.
Luthey-Schulten
Z A
ZA
Wolynes
P G
PG
D000596:Amino Acids; D000818:Animals; D006801:Humans; D008433:Mathematics; D008962:Models, Theoretical; D017510:Protein Folding; D017434:Protein Structure, Tertiary
D000596:Amino Acids