Abstract
Thermodynamics of protein denaturation has been investigated by calorimetry. Analyzing the excess heat capacity curve of a protein obtained using an adiabatic differential scanning calorimeter, we can get important thermodynamic parameters of protein denaturation such as heat capacity change of denaturation and temperature functions of denaturation enthalpy, denaturation entropy, and denaturation Gibbs energy. In this paper, the thermodynamic parameters have been discussed to elucidate the role of each amino acid residue in conformational stability of a protein.
