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J Proteomics. 2012 Feb 16;75(5):1654-65. doi: 10.1016/j.jprot.2011.12.003. Epub 2011 Dec 11.

Predict and analyze S-nitrosylation modification sites with the mRMR and IFS approaches.

Author information

1
Key Laboratory of Systems biology, Shanghai Institutes for Biological Science, Chinese Academy of Science, Shanghai 200031, PR China.

Abstract

S-nitrosylation (SNO) is one of the most important and universal post-translational modifications (PTMs) which regulates various cellular functions and signaling events. Identification of the exact S-nitrosylation sites in proteins may facilitate the understanding of the molecular mechanisms and biological function of S-nitrosylation. Unfortunately, traditional experimental approaches used for detecting S-nitrosylation sites are often laborious and time-consuming. However, computational methods could overcome this demerit. In this work, we developed a novel predictor based on nearest neighbor algorithm (NNA) with the maximum relevance minimum redundancy (mRMR) method followed by incremental feature selection (IFS). The features of physicochemical/biochemical properties, sequence conservation, residual disorder, amino acid occurrence frequency, second structure and the solvent accessibility were utilized to represent the peptides concerned. Feature analysis showed that the features except residual disorder affected identification of the S-nitrosylation sites. It was also shown via the site-specific feature analysis that the features of sites away from the central cysteine might contribute to the S-nitrosylation site determination through a subtle manner. It is anticipated that our prediction method may become a useful tool for identifying the protein S-nitrosylation sites and that the features analysis described in this paper may provide useful insights for in-depth investigation into the mechanism of S-nitrosylation.

PMID:
22178444
DOI:
10.1016/j.jprot.2011.12.003
[Indexed for MEDLINE]

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