期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 84, 期 -, 页码 131-144出版社
WILEY
DOI: 10.1002/prot.24943
关键词
CASP; contact prediction; correlated mutations; co-variation; evolutionary coupling
资金
- US National Institute of General Medical Sciences (NIGMS/NIH) [R01GM100482]
- KAUST Award [KUK-I1-012-43]
This article provides a report on the state-of-the-art in the prediction of intra-molecular residue-residue contacts in proteins based on the assessment of the predictions submitted to the CASP11 experiment. The assessment emphasis is placed on the accuracy in predicting long-range contacts. Twenty-nine groups participated in contact prediction in CASP11. At least eight of them used the recently developed evolutionary coupling techniques, with the top group (CONSIP2) reaching precision of 27% on target proteins that could not be modeled by homology. This result indicates a breakthrough in the development of methods based on the correlated mutation approach. Successful prediction of contacts was shown to be practically helpful in modeling three-dimensional structures; in particular target T0806 was modeled exceedingly well with accuracy not yet seen for ab initio targets of this size (>250 residues). (C) 2015 Wiley Periodicals, Inc.
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