INVESTIGATION OF MOLECULAR-MOTION AND INTERPROTEIN INTERACTIONS IN SOLUTIONS BY TDDS - A COMPARISON WITH NMR DATA

The results of dynamic protein behavior in solution studied by time do main dielectric spectroscopy (TDDS) are presented. The analyses for my oglobin solutions at concentrations 50, 120 and 150 mg/ml in the tempe rature interval from 5 to 35 degrees C was carried out in terms of dip ole correlation functions. It was found that the correlation function of the protein motion can be presented as a sum of three components co rresponding to three types of protein motion: internal local motion, a nisotropy rotational Brownian diffusion and translational Brownian dif fusion. 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 i nterprotein electrostatic steering.