Abstract
Scanning microcalorimetry has a remarkable advantage in the study of protein structure, because it gives all information on the thermodynamic states of proteins as enthalpy function. Owing to the development of scanning microcalorimetry, heat capacity functions for thermal transition of small compact globular proteins, multidomein proteins and multisubunit proteins have been precisely studied. These data have revealed general principles for the thermodynamic properties of ordered structure of small globular proteins and for organizing into large protein molecules. In this paper, recent investigations on the following subjects are reviewed; (1) the experimental studies on small proteins such as neurotoxins, (2) theoretical elucidation of the heat capacity difference between native and denatured states, (3) calorimetric data analysis for multi-domein or multi-subunit proteins, and (4) effects of nonspecific interactions between proteins and additives on the protein structure
