Biomolecular stability analysis for the regulated environment

Differential Scanning Calorimetry (DSC) is a powerful analytical technique which characterizes the thermal stability of proteins and other biomolecules.

In solution, these molecules often undergo thermally-induced conformational changes, such as the breaking of non-covalent bonds leading to the unfolding of a protein. These types of structural rearrangement are detectable by DSC as they require the absorption of energy in the form of heat.

Even in dilute solutions of protein, the new MicroCal PEAQ-DSC systems detect such heat changes and use them to accurately characterize the thermal stability of the molecule under analysis.