This article is a US Government work and, as such, is in the public domain in the United States of America.
Comparison of Prediction Quality in Three CASPS
Some measures of comparative performance in the three CASPs†
Article first published online: 8 NOV 1999
DOI: 10.1002/(SICI)1097-0134(1999)37:3+<231::AID-PROT30>3.0.CO;2-1
Published 1999 Wiley-Liss, Inc.
Issue
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Proteins: Structure, Function, and Bioinformatics
Supplement: Third Meeting on the Critical Assessment of Techniques for Protein Structure Prediction
Volume 37, Issue Supplement 3, pages 231–237, 1999
Additional Information
How to Cite
Venclovas, Č., Zemla, A., Fidelis, K. and Moult, J. (1999), Some measures of comparative performance in the three CASPs. Proteins, 37: 231–237. doi: 10.1002/(SICI)1097-0134(1999)37:3+<231::AID-PROT30>3.0.CO;2-1
- †
Publication History
- Issue published online: 8 NOV 1999
- Article first published online: 8 NOV 1999
- Manuscript Accepted: 15 JUN 1999
- Manuscript Received: 10 JUN 1999
Funded by
- DOE. Grant Number: DE-FG02-96ER62271
- Abstract
- Article
- References
- Cited By
Keywords:
- protein structure prediction;
- community wide experiment;
- CASP
Abstract
Performance in the three Critical Assessment of protein Structure Prediction (CASP) experiments has been compared in the areas of alignment accuracy for models based on homology and three-dimensional accuracy for models produced by using ab initio prediction methods. The homologous models span the comparative modeling and fold-recognition regimes. Each CASP target is assigned a relative difficulty based on the extent of sequence identity and the degree of structural overlap with the best available template. There is a clear improvement in alignment accuracy between CASP1 and CASPs 2 and 3 over much of the difficulty scale but no apparent improvement between CASP2 and CASP3. Encouragingly, the best ab initio models of small targets are clearly more accurate in CASP3 than in CASPs 1 and 2. Proteins Suppl 1999;3:231–237. Published 1999 Wiley-Liss, Inc.

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