Mechanical Stability of Ribonuclease A Heavily Depends on the Redox Environment.

ABSTRACT: Disulfide bonds are covalent bonds that connect nonlocal fragments of proteins, and they are unique post-translational modifications of proteins. They require the oxidizing environment to be stable, which occurs for example during oxidative stress; however, in a cell the reductive environment is maintained, lowering their stability. Despite many years of research on disulfide bonds, their role in the protein life cycle is not fully understood and seems to strictly depend on a system or process in which they are involved. In this article, coarse-grained UNited RESidue (UNRES), and all-atom Assisted Model Building with Energy Refinement (AMBER) force fields were applied to run a series of steered molecular dynamics (SMD) simulations of one of the most studied, but still not fully understood,

SUBMITTER: Smardz P 

PROVIDER: S-EPMC9421896 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature