The use of TDDS for investigation of structural and dynamic behavior of protein molecules in aqueous solution

The use of time domain dielectric spectroscopy (TDDS) for the investigation of protein structure and dynamic behavior in solution seems to us suitable since this method permits us to obtain the information about the relaxation processes, associated with the intramolecular motions and Brownian tumbling as a whole. It is known that in the native state the protein represents a reasonably rigid packed globule. However, under the effect of external conditions, the structure of protein can undergo essential changes. Under the influence of temperature, denaturants, pH of solution, etc., the globule structure can be transformed into a disordered coil. The applications of TDDS measurements to dynamic structure investigation during different conformational transitions of proteins are presented