Molecular dynamic study of SARS-CoV-2 with various S protein mutations and their effect on thermodynamic properties.

ABSTRACT: Studying the structure of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S) protein is important to understand the infection process. The S protein is necessary in completing the virus life cycle and is responsible for the appearance of new variants and drug and vaccine resistance. Understanding the structure and dynamics of biological macromolecules is essential for understanding how they function. In this work, we investigated the effects of mutations on S protein stability and solubility through molecular dynamic (MD) simulation in a 100 ns (ns) period. We screened four variants in addition to the wild type (WT). Results show that changes on MD simulation parameters of S protein indicate fluctuations and changes in the conformation, especially in the area between 30

SUBMITTER: Abdalla M 

PROVIDER: S-EPMC8576119 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature