Comparative Analysis of Dynamic Features of Endolysins T5 and PlyG In Silico

IF 4.033 Q4 Biochemistry, Genetics and Molecular Biology
A. G. Arakelian, G. N. Chuev, T. V. Mamedov, A. Arikov, K. R. Ismailov
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引用次数: 0

Abstract

Bacteriophage endolysins are part of a complex of lytic enzymes responsible for the destruction of peptidoglycan in the bacterial cell wall. The dynamic features of single-domain endolysin of bacteriophage T5 and multi-domain endolysin PlyG of gamma phage have been studied by methods of molecular dynamics and normal mode analysis. The nature of activation of bacteriophage T5 endolysins by calcium and a discovered fundamental difference in the dynamic features of single-domain and multi-domain endolysins are explained.

Abstract Image

Abstract Image

硅内溶素T5和PlyG动态特性的比较分析
噬菌体内溶素是负责破坏细菌细胞壁肽聚糖的分解酶复合体的一部分。采用分子动力学和正态分析方法研究了噬菌体T5单域内溶素和γ噬菌体PlyG多域内溶素的动态特性。本文解释了钙活化噬菌体T5内溶素的性质,以及发现的单域和多域内溶素动态特性的根本差异。
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来源期刊
Biophysics
Biophysics Biochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
1.20
自引率
0.00%
发文量
67
期刊介绍: Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.
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