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PMID: 14579346 Published · ppublish English Journal Article

Evaluation of disorder predictions in CASP5.

Proteins ·Vol. 53 Suppl 6 ·2003-00-00 ·Pages 561-5

Melamud E, Moult J

Abstract

This paper reports an analysis of the accuracy of predictions of structural disorder received as part of the CASP5 experiment. Six groups made predictions of disorder. The predictions of the four most active groups have been compared with the experimental results, in terms of the sensitivity and specificity of the methods. All four methods succeed in detecting over half the disordered residues in the targets, with a generally low rate of over-prediction. Two of the methods perform significantly better when the structure of a related protein is available. There is a trade-off between the fraction of disordered residues detected and the extent of over-prediction, and groups have adopted different compromises in this respect. Comparison of performance at the same over-prediction rates highlights the role of related structures in some methods rather than others, with different groups achieving the highest sensitivity for different target sets. Over-all, the methods are clearly of considerable use in identifying potential disorder.

MeSH Terms
Computational Biology/methods,standards Protein Conformation Protein Folding Proteins/chemistry Reproducibility of Results Sensitivity and Specificity
Chemicals
Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Melamud Eugene
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA.
Moult John
Article Info
Journal
Proteins
Abbr.
Proteins
ISSN
1097-0134
Published
2003-00-00
Pages
561-5
Language
English
Region
United States
NLM ID
8700181
Subset
IM
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