TY - JOUR
T1 - New encouraging developments in contact prediction: Assessment of the CASP11 results
AU - Monastyrskyy, Bohdan
AU - D'Andrea, Daniel
AU - Fidelis, Krzysztof
AU - Tramontano, Anna
AU - Kryshtafovych, Andriy
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: Grant sponsor: US National Institute of General Medical Sciences (NIGMS/NIH);Grant number: R01GM100482; Grant sponsor: KAUST Award; Grant number:KUK-I1-012-43.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.
PY - 2015/11/17
Y1 - 2015/11/17
N2 - © 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).
AB - © 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).
UR - http://hdl.handle.net/10754/598971
UR - http://doi.wiley.com/10.1002/prot.24943
UR - http://www.scopus.com/inward/record.url?scp=84947707636&partnerID=8YFLogxK
U2 - 10.1002/prot.24943
DO - 10.1002/prot.24943
M3 - Article
C2 - 26474083
SN - 0887-3585
VL - 84
SP - 131
EP - 144
JO - Proteins: Structure, Function, and Bioinformatics
JF - Proteins: Structure, Function, and Bioinformatics
ER -