Differential Scanning Calorimetry and Protein Stability

Differential scanning calorimetry (DSC) is a technique applicable to the study of protein stability. It measures the excess heat capacity of a protein relative to a reference sample. Deconvolution of a thermogram can provide insight in the unfolding process and about the presence of stable intermediate states. From the denaturation curve of a protein all the important thermodynamical parameters can be obtained. Protein fluorescence and circular dichroism (CD) on the other hand are spectral techniques, which can monitor the changes in the tertiary and secondary structure. The studies reviewed in this article demonstrate that DSC is a useful technique for studying protein denaturation and protein-ligand interactions. Especially the combination of DSC with a spectral technique appeared to be a very powerful in protein research.