0 ERMOLINA, I FEDOTOV, V FELDMAN, Y IVOYLOV, I 1994 JOURNAL OF NON-CRYSTALLINE SOLIDS 172 1103-1108 SEP The results of dynamic protein behavior in solution studied by time domain dielectric spectroscopy (TDDS) are presented. The analyses for myoglobin solutions at concentrations 50, 120 and 150 mg/ml in the temperature interval from 5 to 35 degrees C was carried out in terms of dipole correlation functions. It was found that the correlation function of the protein motion can be presented as a sum of three components corresponding to three types of protein motion: internal local motion, anisotropy rotational Brownian diffusion and translational Brownian diffusion. According to the hypothesis presented earlier, it is supposed that the reason for anisotropy of protein rotation and capability for the detection translational diffusion (slowest motion) is the mutual interprotein electrostatic steering.