Type
ArticleKAUST Grant Number
KUK-I1-012-43Date
2011-09-16Online Publication Date
2011-09-16Print Publication Date
2011Permanent link to this record
http://hdl.handle.net/10754/598246
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Lack of stable three-dimensional structure, or intrinsic disorder, is a common phenomenon in proteins. Naturally, unstructured regions are proven to be essential for carrying function by many proteins, and therefore identification of such regions is an important issue. CASP has been assessing the state of the art in predicting disorder regions from amino acid sequence since 2002. Here, we present the results of the evaluation of the disorder predictions submitted to CASP9. The assessment is based on the evaluation measures and procedures used in previous CASPs. The balanced accuracy and the Matthews correlation coefficient were chosen as basic measures for evaluating the correctness of binary classifications. The area under the receiver operating characteristic curve was the measure of choice for evaluating probability-based predictions of disorder. The CASP9 methods are shown to perform slightly better than the CASP7 methods but not better than the methods in CASP8. It was also shown that capability of most CASP9 methods to predict disorder decreases with increasing minimum disorder segment length.Citation
Monastyrskyy B, Fidelis K, Moult J, Tramontano A, Kryshtafovych A (2011) Evaluation of disorder predictions in CASP9. Proteins: Structure, Function, and Bioinformatics 79: 107–118. Available: http://dx.doi.org/10.1002/prot.23161.Sponsors
Grant sponsor: US National Library of Medicine (NIH/NLM); Grant number: LM007085; Grant sponsor: King Abdullah University of Science and Technology (KAUST); Grant number: KUK-I1-012-43.Publisher
WileyPubMed ID
21928402PubMed Central ID
PMC3212657ae974a485f413a2113503eed53cd6c53
10.1002/prot.23161
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