iProtGly‐SS: Identifying protein glycation sites using sequence and structure based features

Glycation is chemical reaction by which sugar molecule bonds with a protein without the help of enzymes. This is often cause to many diseases and therefore the knowledge about glycation is very important. In this paper, we present iProtGly‐SS, a protein lysine glycation site identification method ba...

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Veröffentlicht in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2018-07, Vol.86 (7), p.777-789
Hauptverfasser: Islam, Md Mofijul, Saha, Sanjay, Rahman, Md Mahmudur, Shatabda, Swakkhar, Farid, Dewan Md, Dehzangi, Abdollah
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Sprache:eng
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Zusammenfassung:Glycation is chemical reaction by which sugar molecule bonds with a protein without the help of enzymes. This is often cause to many diseases and therefore the knowledge about glycation is very important. In this paper, we present iProtGly‐SS, a protein lysine glycation site identification method based on features extracted from sequence and secondary structural information. In the experiments, we found the best feature groups combination: Amino Acid Composition, Secondary Structure Motifs, and Polarity. We used support vector machine classifier to train our model and used an optimal set of features using a group based forward feature selection technique. On standard benchmark datasets, our method is able to significantly outperform existing methods for glycation prediction. A web server for iProtGly‐SS is implemented and publicly available to use: http://brl.uiu.ac.bd/iprotgly-ss/.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.25511