Prediction of Protein-Protein Interaction Using Distance Frequency of Amino Acids Grouped with their Physicochemical Properties

Shaowu Zhang, Yong-mei Cheng, Li Luo, Q. Pan
{"title":"Prediction of Protein-Protein Interaction Using Distance Frequency of Amino Acids Grouped with their Physicochemical Properties","authors":"Shaowu Zhang, Yong-mei Cheng, Li Luo, Q. Pan","doi":"10.1109/BIC-TA.2011.53","DOIUrl":null,"url":null,"abstract":"Protein-protein interactions (PPIs) play a key role in many cellular processes. These interactions form the basis of phenomena such as DNA replication and transcription, metabolic pathway, signaling pathway, and cell cycle control. Knowing how proteins interact with each other can help the biological scientist understand the molecular mechanism of the cell. Unfortunately, the experimental methods of identifying PPIs are both time-consuming and expensive. Therefore, developing computational approaches for predicting PPIs would be of significant value. Here, we propose a novel method for predicting the PPI using distance frequency of amino acids grouped with their physicochemical properties (hydrophobicity, normalized van der Waals volume, polarity and polarizability) and PCA. First, the 20 basic amino acids were divided into three groups according to the four kinds of physicochemical property values. Second, the distance frequency feature extraction method was introduced to represent the protein pairs, and also fused the feature vectors extracted with four physicochemical properties to form different feature vector sets. Third, the PCA method was used to reduce the vector dimension, and support vector machine was adopted as the classifier. The overall success rate of our method for hydrophobicity, normalized van der Waals volume, polarity and polarizability are 89.88%, 89.72%, 89.28% and 89.24% in 10CV test, which are 6.65%, 8.05%, 9.72% and 8.09% higher than that of Guo's auto-covariance function feature extraction method respectively. The total predicting accuracy of fusing the four physicochemical properties arrives at 91.79%. The results show that the current approach is very promising for predicting PPI, and may become a useful tool in the relevant areas.","PeriodicalId":211822,"journal":{"name":"2011 Sixth International Conference on Bio-Inspired Computing: Theories and Applications","volume":"26 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2011-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"2011 Sixth International Conference on Bio-Inspired Computing: Theories and Applications","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/BIC-TA.2011.53","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 4

Abstract

Protein-protein interactions (PPIs) play a key role in many cellular processes. These interactions form the basis of phenomena such as DNA replication and transcription, metabolic pathway, signaling pathway, and cell cycle control. Knowing how proteins interact with each other can help the biological scientist understand the molecular mechanism of the cell. Unfortunately, the experimental methods of identifying PPIs are both time-consuming and expensive. Therefore, developing computational approaches for predicting PPIs would be of significant value. Here, we propose a novel method for predicting the PPI using distance frequency of amino acids grouped with their physicochemical properties (hydrophobicity, normalized van der Waals volume, polarity and polarizability) and PCA. First, the 20 basic amino acids were divided into three groups according to the four kinds of physicochemical property values. Second, the distance frequency feature extraction method was introduced to represent the protein pairs, and also fused the feature vectors extracted with four physicochemical properties to form different feature vector sets. Third, the PCA method was used to reduce the vector dimension, and support vector machine was adopted as the classifier. The overall success rate of our method for hydrophobicity, normalized van der Waals volume, polarity and polarizability are 89.88%, 89.72%, 89.28% and 89.24% in 10CV test, which are 6.65%, 8.05%, 9.72% and 8.09% higher than that of Guo's auto-covariance function feature extraction method respectively. The total predicting accuracy of fusing the four physicochemical properties arrives at 91.79%. The results show that the current approach is very promising for predicting PPI, and may become a useful tool in the relevant areas.
根据理化性质分组的氨基酸距离频率预测蛋白质-蛋白质相互作用
蛋白质-蛋白质相互作用(PPIs)在许多细胞过程中起着关键作用。这些相互作用构成了DNA复制和转录、代谢途径、信号通路和细胞周期控制等现象的基础。了解蛋白质如何相互作用可以帮助生物科学家了解细胞的分子机制。不幸的是,鉴定ppi的实验方法既耗时又昂贵。因此,开发预测ppi的计算方法将具有重要的价值。在这里,我们提出了一种新的方法来预测PPI使用氨基酸的距离频率分组的物理化学性质(疏水性,归一化范德华体积,极性和极化率)和PCA。首先,根据4种理化性质值将20种碱性氨基酸分为3类。其次,引入距离频率特征提取方法来表示蛋白质对,并将提取的四种理化性质特征向量融合形成不同的特征向量集;第三,采用主成分分析方法降维向量,采用支持向量机作为分类器。在10CV测试中,我们的方法对疏水性、归一化范德华体积、极性和极化率的总体成功率分别为89.88%、89.72%、89.28%和89.24%,分别比Guo的自协方差函数特征提取方法高6.65%、8.05%、9.72%和8.09%。融合四种物化性质的总预测精度达到91.79%。结果表明,目前的方法对PPI的预测是非常有希望的,并可能成为相关领域的有用工具。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信