Evaluation of disorder predictions in CASP9

Bohdan Monastyrskyy, Krzysztof Fidelis, John Moult, Anna Tramontano, Andriy Kryshtafovych

Research output: Contribution to journalArticlepeer-review

97 Scopus citations


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.
Original languageEnglish (US)
Pages (from-to)107-118
Number of pages12
JournalProteins: Structure, Function, and Bioinformatics
Issue numberS10
StatePublished - Sep 16 2011
Externally publishedYes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: 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.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.


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