Slaving: Solvent fluctuations dominate protein dynamics and functions

摘要: Protein motions are essential for function. Comparing protein processes with the dielectric fluctuations of surrounding solvent shows that they fall into two classes: nonslaved and slaved. Nonslaved independent motions; their rates determined by conformation vibrational dynamics. Slaved tightly coupled to solvent; have approximately same temperature dependence as rate fluctuations, but smaller. Because is activation enthalpy, we propose responsible whereas hydration shell control entropy through energy landscape. Bond formation prototype processes; opening closing channels quintessential slaved motions. The prevalence highlights importance environment in cells membranes function proteins.