Isothermal Titration Calorimetry (ITC) is the gold standard for measuring biomolecular interactions.  ITC simultaneously determines all binding parameters (n, K, ∆H and ΔS) in a single experiment – information that cannot be obtained from any other method.

When substances bind, heat is either generated or absorbed.  ITC is a thermodynamic technique that directly measures the heat released or absorbed during a biomolecular binding event.  Measurement of this heat allows accurate determination of binding constants (K), reaction stoichiometry (n), enthalpy (∆H) and entropy (ΔS), thereby providing a complete thermodynamic profile of the molecular interaction in a single experiment.  Because ITC goes beyond binding affinities and can elucidate the mechanism of the molecular interaction, it has become the method of choice for characterizing biomolecular interactions.

Applications include:

• Characterization of molecular interactions of small molecules, proteins, antibodies, nucleic acids, lipids and other biomolecules.
• Lead optimization.
• Enzyme kinetics.
• Assessment of the effect of molecular structure changes on binding mechanisms.
• Assessment of biological activity.

• Interactions between any two molecules can be studied with ITC, including:

• Protein-small molecule
• Protein-protein
• Target-drug
• Enzyme-inhibitor
• Antibody-antigen
• Protein-DNA
• Protein-lipid
• Small molecule-small molecule

Please e-mail Mandar_Naik@Brown.edu to gain the ability to book an instrument through our calendar system.

To view the availability of this instrument, please click on the link below:

Microcal ITC200