Studies of the Protein Molecule by Differential Scanning Microcalorimetry

Recent developments of differential adiabatic scanning microcalorimetry have been permitted the precise measurements of the slight changes in heat capacity of the dilute protein solution which is caused by the transition of the higher order protein structure. As the most important feature of the calorimetry is the direct observation of thermodynamic functions, it is an effective measurement for the thermal stability and fluctuation of protein molecule. In this article, a brief review on the basic principle of the calorimetry and new statistical thermodynamic methods for the calorimetry data analysis, by which thermodynamic characteristics of globular proteins have been well recognized, is presented. Cold denaturation and multistate transition of protein molecule are mentioned.