Osmolyte-induced protein stability changes explained by graph theory.

ABSTRACT: Enhanced stabilization of protein structures via the presence of inert osmolytes is a key mechanism adopted both by physiological systems and in biotechnological applications. While the intrinsic stability of proteins is ultimately fixed by their amino acid composition and organization, the interactions between osmolytes and proteins together with their concentrations introduce an additional layer of complexity and in turn, a method of modulating protein stability. Here, we combined experimental measurements with molecular dynamics simulations and graph-theory-based analyses to predict the stabilizing/destabilizing effects of different kinds of osmolytes on proteins during heat-mediated denaturation. We found that (i) proteins in solution with stability-enhancing osmolytes tend to have mor

SUBMITTER: Miotto M 

PROVIDER: S-EPMC11630646 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature