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Analysis of relevant physicochemical properties in obligate and non-obligate protein-protein interactions

机译:专性和非专性蛋白质-蛋白质相互作用的相关理化性质分析

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Identification and analysis of types of protein-protein interactions (PPI) is an important problem in molecular biology because of its key role in many biological processes in living cells. In this paper, we focus on obligate and non-obligate complexes, their prediction and analysis. We propose a feature selection scheme called MRMRpro which is based on Minimum Redundancy Maximum Relevance (MRMR) to focus on the most discriminative and relevant properties to distinguish between these two types of complexes. Our prediction approach uses desolvation energies of pairs of atoms or amino acids present in the interfaces of such complexes. Our results on two well-known datasets confirm that MRMRpro leads to significant improvements on performance by finding more relevant features for prediction. Furthermore, the prediction performance of our biologically guided feature selection methods demonstrate that hydrophobic amino acids are more discriminating than hydrophilic and amphipathic amino acids to distinguish between obligate and non-obligate complexes.
机译:蛋白质-蛋白质相互作用(PPI)类型的鉴定和分析是分子生物学中的一个重要问题,因为它在活细胞的许多生物学过程中起着关键作用。在本文中,我们专注于专性和非专性复合物,它们的预测和分析。我们提出了一种称为MRMR pro 的特征选择方案,该方案基于最小冗余最大相关性(MRMR)来关注于最具区分性和相关性的属性,以区分这两种类型的复合体。我们的预测方法使用了此类复合物界面中存在的成对的原子或氨基酸的去溶剂化能。我们在两个著名的数据集上的结果证实了MRMR pro 通过找到更多相关的预测特征可以显着提高性能。此外,我们生物学指导的特征选择方法的预测性能表明,疏水性氨基酸比亲水性和两亲性氨基酸更具区分性,可以区分专性和非专性复合物。

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