TABLE 3.

Thermodynamic parameters for the binding of the wild-type Keap1-DC and Keap1-DC R415K to the ETGE peptide (Leu-76 to Leu-84) of the Neh2 domain at 25°Ca

Keap1-DCncKab (106 M−1)ΔHb (kcal/mol)TΔSb (kcal/mol)ΔGb (kcal/mol)
Wild type0.98 ± 0.045.5 ± 0.3−14.8 ± 0.3−5.6 ± 0.3−9.2 ± 0.0
R415K0.92 ± 0.000.5 ± 0.1−6.4 ± 0.31.4 ± 0.3−7.8 ± 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.