Malik Shamita, Sharma Dolly, Khatri Sunil Kumar
Amity School of Engineering and Technology, Amity University, Uttar Pradesh, India.
Computer Science and Engineering Department, Shiv Nadar University, Uttar Pradesh, India.
IET Nanobiotechnol. 2017 Dec;11(8):1005-1016. doi: 10.1049/iet-nbt.2016.0177.
In this study, a novel substitution method for finding potential protein-protein interactions (PPIs) has been discussed. This newly designed method for analyzing PPI also aids in the comparison of evolutionary distances. The method deals with various data sets, and additionally performs measurable assessment to determine PPIs is introduced. PPIs are biologically relevant and aid in better conceptual framework of phylogenetic profiling. The newly designed framework gives vision to relate the topological properties of the system with evolutionary behavior of datasets. Firstly, this study found that the most conserved protein motifs exist at the roots of the system, whereas newer motifs with mutations have a tendency to dwell on the branches. In-depth functional analysis revealed that the most conserved motifs have high specificity for improved structural procedures and pathway engagements, which may help identify their formative parts in cells. In conclusion, this study demonstrates several important aspects for future studies focusing to enhance phylogenetic profiling systems. This study can also be used effectively to utilize such strategies to develop new biological insights which will further lead to understanding of disease mechanisms.
在本研究中,讨论了一种用于寻找潜在蛋白质-蛋白质相互作用(PPI)的新型替代方法。这种新设计的分析PPI的方法也有助于比较进化距离。该方法处理各种数据集,并引入了用于确定PPI的可测量评估。PPI具有生物学相关性,有助于构建更好的系统发育谱概念框架。新设计的框架使人们能够将系统的拓扑特性与数据集的进化行为联系起来。首先,本研究发现最保守的蛋白质基序存在于系统的根部,而带有突变的新基序倾向于存在于分支上。深入的功能分析表明,最保守的基序对改善结构过程和途径参与具有高度特异性,这可能有助于识别它们在细胞中的形成部分。总之,本研究展示了未来致力于增强系统发育谱系统的研究的几个重要方面。本研究还可以有效地用于利用此类策略来开发新的生物学见解,这将进一步有助于理解疾病机制。