| Literature DB >> 14579348 |
David T Jones1, Jonathan J Ward.
Abstract
We describe here the results of using a neural network based method (DISOPRED) for predicting disordered regions in 55 proteins in the 5(th) CASP experiment. A set of 715 highly resolved proteins with regions of disorder was used to train the network. The inputs to the network were derived from sequence profiles generated by PSI-BLAST. A post-filter was applied to the output of the network to prevent regions being predicted as disordered in regions of confidently predicted alpha helix or beta sheet structure. The overall two-state prediction accuracy for the method is very high (90%) but this is highly skewed by the fact that most residues are observed to be ordered. The overall Matthews' correlation coefficient for the submitted predictions is 0.34, which gives a more realistic impression of the overall accuracy of the method, though still indicates significant predictive power. Copyright 2003 Wiley-Liss, Inc.Entities:
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Year: 2003 PMID: 14579348 DOI: 10.1002/prot.10528
Source DB: PubMed Journal: Proteins ISSN: 0887-3585