PMC:1635054 / 864-1592 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/1635054","sourcedb":"PMC","sourceid":"1635054","source_url":"https://www.ncbi.nlm.nih.gov/pmc/1635054","text":"The proposed TS heuristic with a novel tabu definition generally performs better than MCS for this problem. Our experiments show that, at least for small proteins (up to 35 amino acids), it is possible to reconstruct the protein backbone solely from the HSE or CN information. In general, the HSE measure leads to better models than the CN measure, as judged by the RMSD and the angle correlation with the native structure. The angle correlation, a measure of structural similarity, evaluates whether equivalent residues in two structures have the same general orientation. Our results indicate that the HSE measure is potentially very useful to represent solvent exposure in protein structure prediction, design and simulation.","tracks":[]}