TABLE 2.
Thermodynamic parameters for binding of DLG mutants to Keap1-DC at 25°Ca
| Alanine mutation | n | Ka (106 M−1) | ΔH (kcal/mol) | TΔS (kcal/mol) | ΔG (kcal/mol) |
|---|---|---|---|---|---|
| D21A | 0.92 ± 0.03 | 1.1 ± 0.0 | −4.4 ± 0.0 | +3.8 ± 0.1 | −8.2 ± 0.0 |
| R25A | 0.97 ± 0.00 | 4.8 ± 0.1 | −8.4 ± 0.0 | +0.7 ± 0.0 | −9.2 ± 0.0 |
| Q26A | 0.96 ± 0.02 | 0.9 ± 0.1 | −4.4 ± 0.2 | +3.7 ± 0.2 | −8.1 ± 0.0 |
| I28A | 0.84 ± 0.01 | 1.3 ± 0.1 | −5.6 ± 0.2 | +2.7 ± 0.3 | −8.3 ± 0.0 |
| L30A | 0.84 ± 0.01 | 0.4 ± 0.0 | −5.4 ± 0.0 | +2.3 ± 0.1 | −7.6 ± 0.0 |
a
n is the stoichiometry, and Ka is the binding constant. ΔH, ΔS, and ΔG are the change in binding enthalpy, entropy, and Gibbs energy, respectively. −RT lnKa = ΔG = ΔH − TΔS, where T and R are the absolute temperature and gas constant, respectively. Values are shown as means ± standard deviations from triplicate runs. The ETGE motif was deleted from all mutants.