Proteins Structure Function and Bioinformatics · 2015 · 91 citations · 47 references
Life SciencesBioinformaticsBiophysicsComputational BiologyStructural BioinformaticsStructural BiologyAb Initio Structure PredictionHomology ModelingProtein StructureProtein Structure ModelingAb Initio Protein ModelingEvolutionary Coupling AnalysisLong-range Contact PredictionLong-range Residue ContactsMutationProtein Contact PredictionResidue-residue Contact PredictionResidue-residue Interactions
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). Proteins 2016; 84(Suppl 1):131-144. © 2015 Wiley Periodicals, Inc.
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