Intermolecular electrostatic interactions and Brownian tumbling in protein solutions.

It is often implicitly assumed that the long-range intermolecular electrostatic interactions in homogeneous protein solutions either are negligible for affecting protein Brownian tumbling or cause its deceleration without changing the shape of rotational auto-correlation function. This review presents a wide set of experimental data (NMR relaxation, dielectric spectroscopy and Brownian dynamics simulations) demonstrating that the interprotein electrostatic steering leads to a complication of the rotational correlation function. The key point of this effect is the rotational anisotropy caused by the interaction of the electric dipole moment of a protein with the external electric field produced by charges of neighboring proteins. Taking this effect into account in some cases might be of critical importance for the correct interpretation of various experimental data.