Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement.

ABSTRACT: The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecular mechanism whereby cosolutes perturb protein stability is still the subject of considerable debate. Probing the molecular details of the cosolvent effect is experimentally challenging as the interactions are very weak and transient, rendering them invisible to most conventional biophysical techniques. Here, we probe cosolute-protein interactions by means of NMR solvent paramagnetic relaxation enhancement together with a formalism we recently developed to quantitatively describe, at atomic resolution, the energetics and dynamics of cosolute-p

SUBMITTER: Okuno Y 

PROVIDER: S-EPMC8403838 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature