TY - JOUR
T1 - Critical assessment of methods of protein structure prediction (CASP) - round x
AU - Moult, John
AU - Fidelis, Krzysztof
AU - Kryshtafovych, Andriy
AU - Schwede, Torsten
AU - Tramontano, Anna
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: Grant sponsor: the US National Institute of General Medical Sciences (NIGMS/NIH); Grant number: R01GM100482 (to KF); Grant sponsors: KAUST Award KUK-I1-012-43 (to AT) and by EMBO.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.
PY - 2013/12/17
Y1 - 2013/12/17
N2 - This article is an introduction to the special issue of the journal PROTEINS, dedicated to the tenth Critical Assessment of Structure Prediction (CASP) experiment to assess the state of the art in protein structure modeling. The article describes the conduct of the experiment, the categories of prediction included, and outlines the evaluation and assessment procedures. The 10 CASP experiments span almost 20 years of progress in the field of protein structure modeling, and there have been enormous advances in methods and model accuracy in that period. Notable in this round is the first sustained improvement of models with refinement methods, using molecular dynamics. For the first time, we tested the ability of modeling methods to make use of sparse experimental three-dimensional contact information, such as may be obtained from new experimental techniques, with encouraging results. On the other hand, new contact prediction methods, though holding considerable promise, have yet to make an impact in CASP testing. The nature of CASP targets has been changing in recent CASPs, reflecting shifts in experimental structural biology, with more irregular structures, more multi-domain and multi-subunit structures, and less standard versions of known folds. When allowance is made for these factors, we continue to see steady progress in the overall accuracy of models, particularly resulting from improvement of non-template regions.
AB - This article is an introduction to the special issue of the journal PROTEINS, dedicated to the tenth Critical Assessment of Structure Prediction (CASP) experiment to assess the state of the art in protein structure modeling. The article describes the conduct of the experiment, the categories of prediction included, and outlines the evaluation and assessment procedures. The 10 CASP experiments span almost 20 years of progress in the field of protein structure modeling, and there have been enormous advances in methods and model accuracy in that period. Notable in this round is the first sustained improvement of models with refinement methods, using molecular dynamics. For the first time, we tested the ability of modeling methods to make use of sparse experimental three-dimensional contact information, such as may be obtained from new experimental techniques, with encouraging results. On the other hand, new contact prediction methods, though holding considerable promise, have yet to make an impact in CASP testing. The nature of CASP targets has been changing in recent CASPs, reflecting shifts in experimental structural biology, with more irregular structures, more multi-domain and multi-subunit structures, and less standard versions of known folds. When allowance is made for these factors, we continue to see steady progress in the overall accuracy of models, particularly resulting from improvement of non-template regions.
UR - http://hdl.handle.net/10754/597894
UR - http://doi.wiley.com/10.1002/prot.24452
UR - http://www.scopus.com/inward/record.url?scp=84893021599&partnerID=8YFLogxK
U2 - 10.1002/prot.24452
DO - 10.1002/prot.24452
M3 - Article
C2 - 24344053
SN - 0887-3585
VL - 82
SP - 1
EP - 6
JO - Proteins: Structure, Function, and Bioinformatics
JF - Proteins: Structure, Function, and Bioinformatics
IS - SUPPL.2
ER -