Function of proteins in biology is closely regulated by their ability to both change their conformation and to provide a fluctuating thermal bath for redox activity. We claim that electrostatics of the protein-water interface, that is both the distribution of the protein surface charge and the polarization of the interfacial waters, is critical for the protein function. Protein conformational fluctuations significantly increase above the temperature of dynamical transition, and that phenomenon is linked to the entrance of the relaxation time of the electric field fluctuations into the instrumental observation window. For redox reactions and photosynthesis, a large breadth of electrostatic fluctuations at the interface provides the driving force for transferring electrons without significant energy losses. These large-scale electrostatic fluctuations are collective in nature and thus occur on time-scales of hundreds of picoseconds to nanoseconds, much longer than single-molecule relaxations times.

Dynamics and statistics of electrostatic fluctuations at the protein-water interface

244th National Meeting (2012)

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