Slaving: Solvent fluctuations dominate protein dynamics and functions
Los Alamos National Laboratory · Technical University of Munich
Abstract
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…
Citation impact
- FWCI
- 9.09
- Percentile
- 100%
- References
- 68
Authors
4- PWPaul W. FenimoreCorresponding
Los Alamos National Laboratory, Technical University of Munich
- HFHans Frauenfelder
Los Alamos National Laboratory, Technical University of Munich
- BHBenjamin H. McMahon
Los Alamos National Laboratory, Technical University of Munich
- FPF. Parak
Los Alamos National Laboratory, Technical University of Munich
Topics & keywords
- Solvent
- Enthalpy
- Chemistry
- Thermodynamics
- Activation energy
- Chemical physics
- Solvent exposure
- Physical chemistry
- Affordable and clean energy