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.
BiophysicsBiochemistry, 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.