Skip to main content

Table 1 Binding affinity constants (KA) and thermodynamic properties of XGBM-carbohydrate interactions*.

From: Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules

Module Carbohydrate
  xyloglucan XXXG XLLG galactose
  K A
(103 M-1)
K A
(103 M-1)
K A
(103 M-1)
ΔG
(kcal mol-1)
ΔH
(kcal mol-1)
TΔS
(kcal mol-1)
n§  
XG-34 ≈ 0.1 ≈ 1 ≈ 1 - - - - not determined
XG-34/1-X ≈ 10 ≈ 1 147 ± 6 -7.0 ± 0.1 -15.8 ± 0.1 -8.8 ± 0.1 1.0 ± 0.0 no binding
XG-34/2-VI ≈ 10 ≈ 1 141 ± 4 -7.0 ± 0.0 -14.0 ± 0.1 -7.0 ± 0.1 1.1 ± 0.0 no binding
  1. *Thermodynamic parameters for some interactions could not be fully characterized due to relatively low affinity, limited solubility of protein and limited availability of ligand. In those cases n was fixed to 1 for data fitting and calculation of KA.
  2. ITC thermograms are available as supplementary information [see Additional file 1]
  3. §calculated number of binding sites on the protein