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    New encouraging developments in contact prediction: Assessment of the CASP11 results

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    Type
    Article
    Authors
    Monastyrskyy, Bohdan
    D'Andrea, Daniel
    Fidelis, Krzysztof cc
    Tramontano, Anna
    Kryshtafovych, Andriy cc
    KAUST Grant Number
    KUK-I1-012-43
    Date
    2015-11-17
    Online Publication Date
    2015-11-17
    Print Publication Date
    2016-09
    Permanent link to this record
    http://hdl.handle.net/10754/598971
    
    Metadata
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    Abstract
    © 2015 Wiley Periodicals, Inc. 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).
    Citation
    Monastyrskyy B, D’Andrea D, Fidelis K, Tramontano A, Kryshtafovych A (2015) New encouraging developments in contact prediction: Assessment of the CASP11 results. Proteins: Structure, Function, and Bioinformatics: n/a–n/a. Available: http://dx.doi.org/10.1002/prot.24943.
    Sponsors
    Grant sponsor: US National Institute of General Medical Sciences (NIGMS/NIH);Grant number: R01GM100482; Grant sponsor: KAUST Award; Grant number:KUK-I1-012-43.
    Publisher
    Wiley
    Journal
    Proteins: Structure, Function, and Bioinformatics
    DOI
    10.1002/prot.24943
    PubMed ID
    26474083
    ae974a485f413a2113503eed53cd6c53
    10.1002/prot.24943
    Scopus Count
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