Process / pipelineThermodynamic Characterization
Isothermal Titration Calorimetry
Isothermal Titration Calorimetry (ITC) is a thermodynamic technique that measures heat released or absorbed during biomolecular binding events at constant temperature. Developed by Wiseman and colleagues in 1989, ITC directly determines binding affinity (Kd), enthalpy (ΔH), and entropy (ΔS) in a single experiment, making it one of the most comprehensive methods for characterizing molecular interactions without requiring labels or immobilization.
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Sources
- Wiseman, T., Williston, S., Brandts, J. F., & Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical Biochemistry, 179(1), 131-137. DOI: 10.1016/0003-2697(89)90213-3 ↗
- Garbett, N. C., & Chaires, J. B. (2012). Binding: A statistical thermodynamic model. Biophysical Journal, 86(6), 3493-3494. DOI: 10.1016/S0006-3495(04)74397-5 ↗