학술논문
Protein tertiary structure recognition using optimized Hamiltonians with local interactions.
Document Type
Article
Source
Proceedings of the National Academy of Sciences of the United States of America; October 1992, Vol. 89 Issue: 19 p9029-9033, 5p
Subject
Language
ISSN
00278424; 10916490
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.