Slaving: solvent fluctuations dominate protein dynamics and functions.
Protein motions are essential for function. Comparing protein processes with the dielectric fluctuations of the surrounding solvent shows that they fall into two classes: nonslaved and slaved. Nonslaved processes are independent of the solvent motions; their rates are determined by the protein conformation and vibrational dynamics. Slaved processes are tightly coupled to the solvent; their rates have approximately the same temperature dependence as the rate of the solvent fluctuations, but they are smaller. Because the temperature dependence is determined by the activation enthalpy, we propose that the solvent is responsible for the activation enthalpy, whereas the protein and the hydration shell control the activation entropy through the energy landscape. Bond formation is the prototype of nonslaved processes; opening and closing of channels are quintessential slaved motions. The prevalence of slaved motions highlights the importance of the environment in cells and membranes for the function of proteins.
Fenimore
P W
PW
Center for Nonlinear Studies, MS B258, and Theoretical Biophysics Group, MS K-710, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Frauenfelder
H
H
McMahon
B H
BH
Parak
F G
FG
D004735:Energy Transfer; D008956:Models, Chemical; D009038:Motion; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000502:physiology*; D012995:Solubility; D012996:Solutions; D012997:Solvents; D013329:Structure-Activity Relationship; D013696:Temperature; D014732:Vibration
D011506:Proteins; D012996:Solutions; D012997:Solvents