Abstract
We report dielectric measurements at radiofrequencies on lysozyme in aqueous solution at two values of pH (3.5 and 6) as a function of temperature in the interval 5–55°C. From the analysis of the dielectric relaxation of the protein solution, the effective hydrodynamic radius r and the electric dipole moment μ of the protein were calculated. The results show that temperature causes continuous gradual changes of r and μ with a maximum at 25–30°C where the Gibbs free energy for native lysozyme shows an analogous trend. We suggest that the gradual variations of r and μ are the manifestation of a redistribution of microscopic state populations of the protein within the same macroscopic native state.
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