Confinement dependence of protein-associated solvent dynamics around different classes of proteins, from the EPR spin probe perspective.

ABSTRACT: Protein function is modulated by coupled solvent fluctuations, subject to the degree of confinement from the surroundings. To identify universal features of the external confinement effect, the temperature dependence of the dynamics of protein-associated solvent over 200-265 K for proteins representative of different classes and sizes is characterized by using the rotational correlation time (detection bandwidth, 10^-10-10^-7 s) of the electron paramagnetic resonance (EPR, X-band) spin probe, TEMPOL, which is restricted to regions vicinal to protein in frozen aqueous solution. Weak (protein surrounded by aqueous-dimethylsulfoxide cryosolvent mesodomain) and strong (no added crysolvent) conditions of ice boundary confinement are imposed. The panel of soluble proteins rep

SUBMITTER: Li W 

PROVIDER: S-EPMC10371532 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature