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Linking thermodynamic parameters to structural and biochemical data allows for a better understanding of substrate binding and its contribution to catalysis. Analyzing the binding of carbohydrates to proteins or enzymes presents a special challenge because of the multiple interactions and forces involved. Isothermal titration calorimetry (ITC) provides a direct measurement of the enthalpy of binding (ΔHa) and allows determination of the binding constant (free energy), entropy and stoichiometry.
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