I. Ermolina et al., INVESTIGATION OF MOLECULAR-MOTION AND INTERPROTEIN INTERACTIONS IN SOLUTIONS BY TDDS - A COMPARISON WITH NMR DATA, Journal of non-crystalline solids, 172, 1994, pp. 1103-1108
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.