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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Brown, H.A., Koropatkin, N.M. (2023). Isothermal Titration Calorimetry for Quantification of Protein–Carbohydrate Interactions. In: Abbott, D.W., Zandberg, W.F. (eds) Carbohydrate-Protein Interactions. Methods in Molecular Biology, vol 2657. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3151-5_9
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DOI: https://doi.org/10.1007/978-1-0716-3151-5_9
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