Characterizing Binding Interactions By ITC

Biochemical reactions are fundamentally driven by processes of recognition, binding, and the formation of non-covalent complexes. Understanding these binding events is crucial for elucidating physiological processes at the molecular level. Consequently, biochemical and biomedical research heavily relies on methodologies that can precisely analyze these binding reactions. One such methodology, Isothermal Titration Calorimetry (ITC), is rapidly gaining prominence as the preferred technique for measuring intermolecular interactions, catalysis, and binding equilibria with exceptional sensitivity. ITC is versatile enough to accurately characterize both low-affinity interactions, such as certain protein-protein interactions, and high-affinity interactions, which include protein-cofactor and enzyme-substrate binding.

This application note highlights the utility of ITC in analyzing non-catalytic macromolecular binding and how ITC can be employed to determine enzyme kinetic parameters, further showcasing its broad applicability in biochemical research.

Access the full application note to learn more.