Isothermal Titration Calorimeter

Model: 

MicroCal PEAQ

TA Instruments NanoITC

Isothermal titration calorimetry (ITC) provides quantitative information on biomolecular interactions via the determination of the thermodynamic parameters of binding. ITC determines binding parameters (n, K, ΔH and ΔS) in a single experiment. 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 (KB), reaction stoichiometry (n), enthalpy (ΔH) and entropy (ΔS), thereby providing a complete thermodynamic profile of the molecular interaction.

Example of 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

Our instrumental capabilities include:

• Directly measure sub-millimolar to nanomolar binding constants (102 to 109 M-1)
• Measure nanomolar to picomolar binding constants (109 to 1012 M-1) using the competitive binding technique.
• The sample cell is 200 µL. As little as 10 µg of protein can be used.

Resources

For excellent notes on setting up samples for ITC, see Vanderbilt University’s Center for Structural Biology ITC page. Note that our instrument is a different model to that described, but the sample preparation notes are relevant.