The use of TDDS for investigation of structural and dynamic behavior of protein molecules in aqueous solution
The results of the investigation of structure and dynamic behavior of protein in solution by time-domain dielectric spectroscopy are presented. The dipole correlation functions for myoglobin, lysozyme and RNase A solutions at different concentration, pH and temperature were obtained. The processes of the intramolecular interactions of myoglobin molecules, the pH-induced dimerization of lysozyme and thermal denaturation of RNase A are discussed.
Citation : Ermolina, I., Fedotov, V. and Feldman, Y. (1998) The use of TDDS for investigation of structural and dynamic behavior of protein molecules in aqueous solution. Physica A, 249 (1-4), pp. 347-352
Research Institute : Leicester Institute for Pharmaceutical Innovation - From Molecules to Practice (LIPI)
Peer Reviewed : Yes
- Leicester School of Pharmacy