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Updated: Apr 30, 2026
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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
Published on: September 7, 2011
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Characterization of molecular interactions using isothermal titration calorimetry
Tino Krell1, Jesús Lacal, Cristina García-Fontana
1Department of Environmental Protection, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, C/Prof. Albareda 1, 18008, Granada, Spain, tino.krell@eez.csic.es.
Methods in Molecular Biology (Clifton, N.J.)
|May 14, 2014
Summary
Isothermal titration calorimetry (ITC) measures heat changes from molecular interactions to determine binding thermodynamics. This versatile technique analyzes various interactions in solution without derivatization.
Area of Science:
- Biochemistry
- Biophysical Chemistry
Background:
- Isothermal titration calorimetry (ITC) is a biophysical technique.
- It quantifies molecular interactions by detecting heat changes during binding events.
Purpose of the Study:
- To explain the principles and applications of Isothermal titration calorimetry (ITC).
- To highlight the utility of ITC in characterizing molecular interactions.
Main Methods:
- ITC involves titrating one molecule against another in solution.
- It measures the heat released or absorbed during the binding process.
Main Results:
- ITC provides a complete set of thermodynamic binding parameters: association/dissociation constants, enthalpy, entropy, and free energy.
- The technique is applicable to a wide range of molecular interactions, including protein-ligand and protein-DNA binding.
- Analysis can be performed in various buffers and temperatures (4-80 °C) without chemical derivatization.
Conclusions:
- ITC is a powerful and versatile tool for characterizing molecular interactions in solution.
- It offers comprehensive thermodynamic data crucial for understanding binding mechanisms.
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