1. iPDA: integrated protein disorder analyzer.
- Author
-
Su CT, Chen CY, and Hsu CM
- Subjects
- Amino Acid Motifs, Amino Acid Sequence, Escherichia coli metabolism, Humans, Molecular Sequence Data, Protein Structure, Secondary, Proteins analysis, Sequence Homology, Amino Acid, Algorithms, Computational Biology methods, Models, Molecular, Proteins chemistry, Sequence Alignment methods, Sequence Analysis, Protein methods, Software
- Abstract
This article presents a web server iPDA, which aims at identifying the disordered regions of a query protein. Automatic prediction of disordered regions from protein sequences is an important problem in the study of structural biology. The proposed classifier DisPSSMP2 is different from several existing disorder predictors by its employment of position-specific scoring matrices with respect to physicochemical properties (PSSMP), where the physicochemical properties adopted here especially take the disorder propensity of amino acids into account. The web server iPDA integrates DisPSSMP2 with several other sequence predictors in order to investigate the functional role of the detected disordered region. The predicted information includes sequence conservation, secondary structure, sequence complexity and hydrophobic clusters. According to the proportion of the secondary structure elements predicted, iPDA dynamically adjusts the cutting threshold of determining protein disorder. Furthermore, a pattern mining package for detecting sequence conservation is embedded in iPDA for discovering potential binding regions of the query protein, which is really helpful to uncovering the relationship between protein function and its primary sequence. The web service is available at http://biominer.bime.ntu.edu.tw/ipda and mirrored at http://biominer.cse.yzu.edu.tw/ipda.
- Published
- 2007
- Full Text
- View/download PDF