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Updated: Jul 31, 2025

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
Published on: September 7, 2011
Isothermal Titration Calorimetry for Quantification of Protein-Carbohydrate Interactions
Haley A Brown1, Nicole M Koropatkin2
1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Abstract:
Isothermal titration calorimetry allows the determination of thermodynamic parameters for the interaction between a protein and mono- or oligosaccharides in solution. For the study of protein-carbohydrate interactions, it is a robust way to determine the stoichiometry and affinity, as well as the enthalpic and entropic contributions to this interaction, without the use of labeled proteins or substrates. Here we describe a standard multiple-injection titration experiment for measuring the binding energetics between a carbohydrate-binding protein and an oligosaccharide.
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