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Prediction of Protein Methylation Sites Using Conditional Random Field

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Protein methylation is an important and reversible post-translational modification which regulates diverse protein properties. Many methylation sites on arginine and lysine have been identification through experiments. However, experimental identification without prior knowledge is laborious and costly. Hence, there is interest in the development of computational methods for reliable prediction of methylation sites. Prediction of methylation sites may provide researches with useful information for further productivity in methylation candidate sites discovery. This work proposes Methcrf, a computational predictor based on conditional random field (CRF) for predicting protein methylation sites limit to lysine and arginine residues due to the absence of enough experimentally verified data for other residues. The approach is developed to consider combining protein sequence features with structural information such as solvent accessibility of amino acids that surround the methylation sites. In 10-fold cross validation Methcrf can achieve the area under receiver operating characteristic curve (AUC) of 0.85 and 0.80 for arginine and lysine, respectively. The proposed method has comparable performance with previous methods for accurately predicting methylation sites.

Keywords: CRF; arginine; cellular plasticity; computational methods; lysine; methylation; post-translational modification; prediction; protein sequence; proteome

Document Type: Research Article


Publication date: January 1, 2013

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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