Characterizing Binding interactions by iTC

All biochemical reactions involve recognition, binding and the formation of noncovalent complexes. Since the characterization of binding events is central to understanding any physiological process at the molecular level, biochemical and biomedical research requires methodologies for precisely analyzing binding reactions. Isothermal titration calorimetry (ITC) is rapidly becoming the method of choice for measuring intermolecular interactions, catalysis and binding equilibria, all with exquisite sensitivity. Both low affinity interactions such as some protein-protein interactions, and high affinity interactions such as protein-cofactor and enzyme-substrate binding, can be quickly and accurately characterized using nanomoles of native (underivatized) sample.