Biological activity of protein depends on their proper structure and stability. Study on macromolecular stability has attracted many scientists. There are many methods to drive the thermodynamic parameters of macromolecules. Differential Scanning Calorimetry (DSC) is unique and powerful tool which directly measures the thermodynamic parameters of macromolecules. Ordinary, thermodynamic parameters are driven based on assumption that there is equilibrium between folded and unfolded state of macromolecules. It is well known that this hypothesis is not valid for most of bio-macromolecules and their unfolding is an irreversible process. From this point of view protein unfolding is kinetically controlled process. For irreversible macromolecules, DSC thermograms are obtained at different scanning rates and protein concentrations. Then curves are analyzed by fitting the data to theoretical equations for the dependence of the excess heat capacity on temperature. In our lecture will have an overview on 3 decades of macromolecular calorimetry in Biophysical Chemistry Lab of Ibb
