| Abstract: | A method has been suggested for obtaining kinetic thermodynamic data on conformational transitions of insoluble proteins by fluorescence measurements. The method was used for treatment of the temperature-induced conformational transition of chymotrypsinogen bonded to the hydroxyethyl methacrylate Spheron matrix. The bonding to Spheron causes destabilization of the native conformation of chymotrypsinogen. Two types of transition of immobilized chymotrypsinogen have been found which are controlled by first-order kinetics with different rate constants. The entropy and enthalpy changes were smaller than for free chymotrypsinogen in solution. The data obtained are interpreted as an effect of the physical interaction of the protein in the activated and denatured states with the polymeric matrix. |
