[Effect of temperature on chymotrypsinogen A hydration in a dynamic system]

The temperature dependence of chymotrypsinogen A was studied by a dynamic method. A gradual exclusion of low adsorbing centers out of the whole number of hydratation centers was observed during the raise of temperature. Differential isosteric heats of hydration were measured at different degrees of hydration. It was shown that at low hydration the heat absorption is connected with the conformational change of the protein molecule.