Predicting Protein Methylation Sites with Physicochemical Properties

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題名:	Predicting Protein Methylation Sites with Physicochemical Properties
作者:	Tsung-Ying Tsai
貢獻者:	Department of Bioinformatics
關鍵詞:	Protein;Mathylation;Post-translational Modification
日期:	2009
上傳時間:	2009-11-06 14:33:45 (UTC+0)
出版者:	Asia University
摘要:	Protein methylation is known as one of reversible post-translational modifications and plays an important role in regulation pathways. Experimental identification of protein methylation sites is in general time-consuming and costs much. Computational approaches to predicting methylation sites provide an efficient way for screening of candidate methylation sites. In this study, hydrophobicity and transfer energy retrieved from the Amino Acid Index database are utilized as the features, and Support Vector machines are employed to perform the classification task. Two training sets are obtained from the MASA dataset, where the numbers of samples, including both 50% positive and 50% negative samples, for modifications of lysine and arginine residues are 266 and 314, respectively. The experimental results are then evaluated by leave-one-out cross validation. The accuracy of predicting lysine residues as the modification sites is up to 79.32%, and 82.8% for the case of arginine residues. The results also show that using these two features mentioned above is simple yet effective in comparison with other features proposed in the literature.
顯示於類別:	[生物資訊與醫學工程學系 ] 博碩士論文

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