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Fuzzy SVM with a Novel Membership Function for Prediction of Protein-Protein Interaction Sites in Homo sapiens

机译:具有新型隶属函数的模糊SVM用于预测智人蛋白质-蛋白质相互作用位点

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Predicting residues that participate in protein-protein interactions (PPI) helps to identify the amino acids located at the interface. In this work, experimentally verified 3-D structures of protein complexes are used for building the training model and subsequent prediction protein interactions from sequence information. Fuzzy SVM (F-SVM), which is developed on top of the classical SVM, is an effective method to solve this problem and we demonstrate that the performance of the SVM can further be improved with the use of a custom-designed fuzzy membership function. We evaluate the performances of both SVM and F-SVM on the PPI database of the Homo sapiens organism and evaluate the statistical significance of F-SVM over classical SVM. To predict interaction sites in protein complexes, local composition of amino acids together with their physico-chemical characteristics are used. The F-SVM based residues prediction method exploits the membership function for each pair sequence fragment and in all cases F-SVM improves the performances obtained by the corresponding SVM classifiers. The F-SVM performance on the test samples is measured by area under ROC curve (AUC) as 80.16% which is around 1.55% higher than the classical SVM classifier.
机译:预测参与蛋白质-蛋白质相互作用(PPI)的残基有助于鉴定位于界面处的氨基酸。在这项工作中,经过实验验证的蛋白质复合物的3-D结构用于构建训练模型,并根据序列信息预测蛋白质的相互作用。在经典SVM的基础上开发的模糊SVM(F-SVM)是解决此问题的有效方法,我们证明了使用定制设计的模糊隶属度函数可以进一步提高SVM的性能。 。我们在智人生物的PPI数据库上评估SVM和F-SVM的性能,并评估F-SVM在经典SVM上的统计意义。为了预测蛋白质复合物中的相互作用位点,使用了氨基酸的局部组成及其理化特性。基于F-SVM的残基预测方法利用了每个对序列片段的隶属度函数,并且在所有情况下F-SVM都会提高由相应SVM分类器获得的性能。测试样品的F-SVM性能通过ROC曲线下的面积(AUC)测得为80.16%,比经典SVM分类器高约1.55%。

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