TABLE 2.

Thermodynamic parameters for the binding of the wild-type Neh2 or Neh2 mutants to Keap1-DC at 25°Ca

Neh2ncKab (107 M−1)ΔHb (kcal/mol)TΔSb (kcal/mol)ΔGb (kcal/mol)
Wild type
    Site 10.49 ± 0.0019.0 ± 4.0−28.4 ± 0.1−17.1 ± 0.1−11.3 ± 0.2
    Site 20.46 ± 0.000.1 ± 0.0−11.2 ± 0.3−3.0 ± 0.3−8.1 ± 0.0
Neh2[Δ1-33]1.01 ± 0.0112.4 ± 0.9−21.2 ± 0.3−10.2 ± 0.2−11.0 ± 0.1
Neh2[ΔETGE]0.94 ± 0.020.2 ± 0.0−6.9 ± 0.31.8 ± 0.3−8.7 ± 0.1
  • a All standard deviations are derived from triplicate runs.

  • b Ka is the binding constant. ΔH, ΔS, and ΔG are the change in binding enthalpy, entropy, and Gibbs energy, respectively. −RTlnKa = ΔG = ΔHTΔS, where T and R are the absolute temperature and the gas constant, respectively.

  • c n, binding stoichiometry.