Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein
- 25 September 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 576 (3) , 348-352
- https://doi.org/10.1016/j.febslet.2004.09.036
Abstract
Intrinsically disordered proteins are an important class of proteins with unique functions and properties. Here, we have applied a support vector machine (SVM) trained on naturally occurring disordered and ordered proteins to examine the contribution of various parameters (vectors) to recognizing proteins that contain disordered regions. We find that a SVM that incorporates only amino acid composition has a recognition accuracy of 87 ± 2%. This result suggests that composition alone is sufficient to accurately recognize disorder. Interestingly, SVMs using reduced sets of amino acids based on chemical similarity preserve high recognition accuracy. A set as small as four retains an accuracy of 84 ± 2%; this suggests that general physicochemical properties rather than specific amino acids are important factors contributing to protein disorder.Keywords
This publication has 28 references indexed in Scilit:
- Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of LifeJournal of Molecular Biology, 2004
- Virtual gating and nuclear transport: the hole pictureTrends in Cell Biology, 2003
- Protein Disorder PredictionStructure, 2003
- Loopy Proteins Appear Conserved in EvolutionJournal of Molecular Biology, 2002
- Natively unfolded proteins: A point where biology waits for physicsProtein Science, 2002
- Statistics of local complexity in amino acid sequences and sequence databasesPublished by Elsevier ,2001
- A novel method of protein secondary structure prediction with high segment overlap measure: support vector machine approach1 1Edited by B. HollandJournal of Molecular Biology, 2001
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999
- Entropic Exclusion by Neurofilament Sidearms: A Mechanism for Maintaining Interfilament SpacingBiochemistry, 1997
- Recognizing Native Folds by the Arrangement of Hydrophobic and Polar ResiduesJournal of Molecular Biology, 1995