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 quickly and accurately characterizing binding interactions without the need to develop new assay protocols for each biomolecule or ligand. Furthermore, ITC’s direct nature and high precision make it invaluable in validating the results of less rigorous, high throughput assay protocols.

The example experiments and analysis in this eBook will help researchers and drug developers apply ITC for reliable and prompt characterization of molecular interactions.

Download to answer:

• How do thermodynamics drive binding and specificity?
• How can I reliably and efficiently quantify intermolecular interactions with ITC?
• How can I measure and control enzymatic functionality and kinetics?
• What physical processes are involved in a binding reaction?
• What thermodynamic processes control the conformational rearrangements necessary to produce the transition state?

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