Applications of Differential Scanning Calorimetry in Studying Folding and Stability of Proteins

Over the last few decades, the analytical method of differential scanning calorimetry (DSC) has been established to investigate the stability, folding, and binding of proteins. The technique typically measures the differential heat between the test and reference samples. The deconvoluted thermogram can provide crucial information on process development and whether there are any stable transition states. Information about all the significant thermodynamical parameters can be extracted from the denaturation curve of a protein. DSC offers several advantages over other spectral methods like fluorescence and circular dichroism (CD) spectroscopy. For instance, CD and fluorescence spectra can only provide information on the secondary structural content of a protein, whereas DSC can be used to study protein stability and different transition states in folding. This chapter summarises the utility of DSC in studying protein stability and folding.