Netsu Sokutei, 34 (1), p. 31, (2007)


Thermodynamic Analysis of Conformational Change Important to Protein Function

In the present post-genome era, although many three-dimensional structures of proteins have been determined at atomic resolution mainly by X-ray structural analysis, there remain some problems, such as dynamic properties of proteins and hydration effects, to clarify the correlation between protein structure and function. Proteins are flexible and need some conformational changes to recognize other molecules, but it is difficult to detect the dynamic properties only by static structural analyses. Thermodynamic analyses of biomolecular interactions reveal details of the energetic and dynamic features of molecular recognition processes, and complement the structural information. I have investigated several biomolecular interactions, including DNA-protein, antigen-antibody, and peptide-protein interactions, using isothermal titration and differential scanning calorimetries, together with other methods, such as NMR, X-ray, and surface plasmon resonance. Here, I focus on the thermodynamics to detect conformational changes of proteins, which is important for biomolecular function in general.