Source:
JOURNAL OF NON-CRYSTALLINE SOLIDS, Volume 172, Number Part 2, p.1103-1108 (1994)
Abstract:
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.
