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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