期刊
STRUCTURE
卷 19, 期 8, 页码 1182-1191出版社
CELL PRESS
DOI: 10.1016/j.str.2011.05.004
关键词
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资金
- Alfred P. Sloan Foundation
- NSF [DBI 1027394]
- National Institute of General Medical Sciences [GM083107, GM084222]
- Hungarian Scientific Research Fund (OTKA) [PD73096]
Although residue-residue contact maps dictate the topology of proteins, sequence-based ab initio contact predictions have been found little use in actual structure prediction due to the low accuracy. We developed a composite set of nine SVM-based contact predictors that are used in I-TASSER simulation in combination with sparse template contact restraints. When testing the strategy on 273 nonhomologous targets, remarkable improvements of I-TASSER models were observed for both easy and hard targets, with p value by Student's t test <0.00001 and 0.001, respectively. In several cases, template modeling score increases by >30%, which essentially converts nonfoldable targets into foldable ones. In CASP9, I-TASSER employed ab initio contact predictions, and generated models for 26 FM targets with a GDT-score 16% and 44% higher than the second and third best servers from other groups, respectively. These findings demonstrate a new avenue to improve the accuracy of protein structure prediction especially for free-modeling targets.
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