Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.

Pyrrolidone carboxylic acid (PCA) is formed during a common post-translational modification (PTM) of extracellular and multi-pass membrane proteins. In this study, we developed a new predictor to predict the modification sites of PCA based on maximum relevance minimum redundancy (mRMR) and increment...

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Main Authors: Lu-Lu Zheng, Shen Niu, Pei Hao, Kaiyan Feng, Yu-Dong Cai, Yixue Li
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3235115?pdf=render
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spelling doaj-0473d09d6a474b16b8d3a6caa9e4e0e52020-11-25T01:53:32ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01612e2822110.1371/journal.pone.0028221Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.Lu-Lu ZhengShen NiuPei HaoKaiyan FengYu-Dong CaiYixue LiPyrrolidone carboxylic acid (PCA) is formed during a common post-translational modification (PTM) of extracellular and multi-pass membrane proteins. In this study, we developed a new predictor to predict the modification sites of PCA based on maximum relevance minimum redundancy (mRMR) and incremental feature selection (IFS). We incorporated 727 features that belonged to 7 kinds of protein properties to predict the modification sites, including sequence conservation, residual disorder, amino acid factor, secondary structure and solvent accessibility, gain/loss of amino acid during evolution, propensity of amino acid to be conserved at protein-protein interface and protein surface, and deviation of side chain carbon atom number. Among these 727 features, 244 features were selected by mRMR and IFS as the optimized features for the prediction, with which the prediction model achieved a maximum of MCC of 0.7812. Feature analysis showed that all feature types contributed to the modification process. Further site-specific feature analysis showed that the features derived from PCA's surrounding sites contributed more to the determination of PCA sites than other sites. The detailed feature analysis in this paper might provide important clues for understanding the mechanism of the PCA formation and guide relevant experimental validations.http://europepmc.org/articles/PMC3235115?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Lu-Lu Zheng
Shen Niu
Pei Hao
Kaiyan Feng
Yu-Dong Cai
Yixue Li
spellingShingle Lu-Lu Zheng
Shen Niu
Pei Hao
Kaiyan Feng
Yu-Dong Cai
Yixue Li
Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.
PLoS ONE
author_facet Lu-Lu Zheng
Shen Niu
Pei Hao
Kaiyan Feng
Yu-Dong Cai
Yixue Li
author_sort Lu-Lu Zheng
title Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.
title_short Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.
title_full Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.
title_fullStr Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.
title_full_unstemmed Prediction of protein modification sites of pyrrolidone carboxylic acid using mRMR feature selection and analysis.
title_sort prediction of protein modification sites of pyrrolidone carboxylic acid using mrmr feature selection and analysis.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2011-01-01
description Pyrrolidone carboxylic acid (PCA) is formed during a common post-translational modification (PTM) of extracellular and multi-pass membrane proteins. In this study, we developed a new predictor to predict the modification sites of PCA based on maximum relevance minimum redundancy (mRMR) and incremental feature selection (IFS). We incorporated 727 features that belonged to 7 kinds of protein properties to predict the modification sites, including sequence conservation, residual disorder, amino acid factor, secondary structure and solvent accessibility, gain/loss of amino acid during evolution, propensity of amino acid to be conserved at protein-protein interface and protein surface, and deviation of side chain carbon atom number. Among these 727 features, 244 features were selected by mRMR and IFS as the optimized features for the prediction, with which the prediction model achieved a maximum of MCC of 0.7812. Feature analysis showed that all feature types contributed to the modification process. Further site-specific feature analysis showed that the features derived from PCA's surrounding sites contributed more to the determination of PCA sites than other sites. The detailed feature analysis in this paper might provide important clues for understanding the mechanism of the PCA formation and guide relevant experimental validations.
url http://europepmc.org/articles/PMC3235115?pdf=render
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AT shenniu predictionofproteinmodificationsitesofpyrrolidonecarboxylicacidusingmrmrfeatureselectionandanalysis
AT peihao predictionofproteinmodificationsitesofpyrrolidonecarboxylicacidusingmrmrfeatureselectionandanalysis
AT kaiyanfeng predictionofproteinmodificationsitesofpyrrolidonecarboxylicacidusingmrmrfeatureselectionandanalysis
AT yudongcai predictionofproteinmodificationsitesofpyrrolidonecarboxylicacidusingmrmrfeatureselectionandanalysis
AT yixueli predictionofproteinmodificationsitesofpyrrolidonecarboxylicacidusingmrmrfeatureselectionandanalysis
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