Table 3 Summary of thermodynamic parameters for ADP-ribose binding

From: Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans

Protein

Kd (µM)

n

ΔH (kJ/mol)

−TΔS (kJ/mol)

ΔG (kJ/mol)

WT

1.78 ± 0.05

1.05 ± 0.05

−89.45 ± 3.08

56.64 ± 3.06

−32.80 ± 0.08

T267R

3.76 ± 0.47

1.09 ± 0.01

−90.44 ± 2.96

59.47 ± 3.26

−30.96 ± 0.30

T267K

1.98 ± 0.02

1.05 ± 0.03

−76.38 ± 0.97

43.84 ± 0.97

−32.53 ± 0.02

E112A

2.02 ± 0.07

1.06 ± 0.04

−40.38 ± 1.59

7.88 ± 1.50

−32.50 ± 0.09

  1. All experiments were carried out at 25 °C. Values are mean plus or minus SEM (n = 3 independent experiments). Plots of raw data and fitted curve are in Supplementary Fig. S16
  2. WT wild type
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