TY - JOUR
T1 - Critical assessment of methods of protein structure prediction (CASP)-round IX
AU - Moult, John
AU - Fidelis, Krzysztof
AU - Kryshtafovych, Andriy
AU - Tramontano, Anna
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: Grant sponsor: National Library of Medicine; Grant number: LM07085; Grant sponsor: NIH Institute of General Medical Sciences; Grant number: GM072354; Grant sponsor: KAUST Award; Grant number: KUK-I1-012-43.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.
PY - 2011/10/14
Y1 - 2011/10/14
N2 - This article is an introduction to the special issue of the journal PROTEINS, dedicated to the ninth 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. Methods for modeling protein structure continue to advance, although at a more modest pace than in the early CASP experiments. CASP developments of note are indications of improvement in model accuracy for some classes of target, an improved ability to choose the most accurate of a set of generated models, and evidence of improvement in accuracy for short "new fold" models. In addition, a new analysis of regions of models not derivable from the most obvious template structure has revealed better performance than expected.
AB - This article is an introduction to the special issue of the journal PROTEINS, dedicated to the ninth 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. Methods for modeling protein structure continue to advance, although at a more modest pace than in the early CASP experiments. CASP developments of note are indications of improvement in model accuracy for some classes of target, an improved ability to choose the most accurate of a set of generated models, and evidence of improvement in accuracy for short "new fold" models. In addition, a new analysis of regions of models not derivable from the most obvious template structure has revealed better performance than expected.
UR - http://hdl.handle.net/10754/597895
UR - http://doi.wiley.com/10.1002/prot.23200
UR - http://www.scopus.com/inward/record.url?scp=80054685109&partnerID=8YFLogxK
U2 - 10.1002/prot.23200
DO - 10.1002/prot.23200
M3 - Article
C2 - 21997831
SN - 0887-3585
VL - 79
SP - 1
EP - 5
JO - Proteins: Structure, Function, and Bioinformatics
JF - Proteins: Structure, Function, and Bioinformatics
IS - S10
ER -