Thermal transitions of proteins

A new method for monitoring the thermal transitions of proteins is described. An unbuffered solution of native protein shows a significant and fairly abrupt change in pH as the protein becomes heat denatured. Suitable plots permit the “melting point” of the protein to be assigned. Twenty proteins have been studied with emphasis on egg albumin. The transition temperature of egg albumin is independent of protein concentration, of pH in the neutral zone, is moderately dependent on the rate of heating, increases with increasing NaCl concentration, varies inversely with the guanidine hydrochloride concentration. There is more than a 35 °C spread in the melting temperatures of the various proteins and no apparent relation exists between the melting temperature of a protein and structural features of the protein.