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Proteins. 2007;69 Suppl 8:129-36.

Assessment of disorder predictions in CASP7.

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  • 1Biozentrum University of Basel, Basel, Switzerland.


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.

(c) 2007 Wiley-Liss, Inc.

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