Assessment of disorder predictions in CASP7

Bordoli, L. and Kiefer, F. and Schwede, T.. (2007) Assessment of disorder predictions in CASP7. Proteins, Vol. 69 Suppl 8. pp. 129-136.

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Official URL: http://edoc.unibas.ch/dok/A5259342

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Intrinsically unstructured regions in proteins have been associated with numerous important biological cellular functions. As measuring native disorder experimentally is technically challenging, computational methods for prediction of disordered regions in a protein have gained much interest in recent years. As part of the seventh Critical Assessment of Techniques for Protein Structure Prediction (CASP7), we have assessed 19 methods for disorder prediction based on their results for 96 target proteins. Prediction accuracy was assessed using detailed numerical comparison between the predicted disorder and the experimental structures. On average, methods participating in CASP7 have improved accuracy in comparison to the previous assessment in CASP6. Overall, however, no improvement over the best methods in CASP6 was observed in CASP7. Significant differences between different prediction methods were identified with regard to their sensitivity and specificity in correctly predicting ordered and disordered residues based on a protein target sequence, which is of relevance for practical applications of these computational tools.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Computational & Systems Biology > Bioinformatics (Schwede)
UniBasel Contributors:Schwede, Torsten
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:21
Deposited On:22 Mar 2012 13:22

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