Figure 5
From: Computational design of a symmetrical β-trefoil lectin with cancer cell binding activity
Isothermal titration calorimetric determination of the affinity of Mitsuba-1 for N-acetyl galactosamine. Fitting to a single-site model with stoichiometry of three sugar ligands to one protein molecule yields a K d value of 0.33 mM. Binding is modestly exothermic under the conditions used, with ΔH of −6.5 kcal/mol, but weakened by the entropy change of −5.8 cal/mol/K.
