Ontology highlight
ABSTRACT:
SUBMITTER: Goldstein RA
PROVIDER: S-EPMC50058 | biostudies-other | 1992 Oct
REPOSITORIES: biostudies-other
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]