Isothermal Titration Calorimetry

ITC measures heats of interactions to characterize macromolecular interactions. We use the technique typically to measure binding constants, enthalpies and entropies of protein-protein and protein-nucleic acid interactions.

Differential Scanning Calorimetry

DSC measures macromolecular stabilities by scanning the heat changes that occur during controlled increase or decrease of temperature. We most often use the technique to observe protein stabilities, protein unfolding, and nucleic acid folding.