Table 2. Thermodynamics of Binding of the DmsA Leader Peptide to DmsDa.
| DmsAL peptide | n | ΔG (kcal/mol) | ΔH (kcal/mol) | –TΔS (kcal/mol) |
|---|---|---|---|---|
| DmsAL21–41 | 1.14 ± 0.09 | –7.4 ± 0.2 | –4.3 ± 0.9 | –3.1 ± 1.1 |
| DmsAL17–41 | 1.04 ± 0.04 | –7.8 ± 0.1 | –9.5 ± 0.8 | 1.7 ± 0.8 |
| DmsAL15–41 | 1.04 ± 0.03 | –8.0 ± 0.1 | –11.7 ± 0.2 | 3.7 ± 0.2 |
| DmsAL15–41 KK | 1.09 ± 0.04 | –7.6 ± 0.1 | –10.0 ± 0.2 | 2.4 ± 0.2 |
a
Thermodynamic parameters were determined from ITC experiments in which each peptide was titrated into a DmsD protein solution at 30 °C and pH 8.0. The mean of triplicate experiments is presented with the corresponding SEM. Values of the Gibbs free energy (ΔG), enthalpy (ΔH), entropy (−TΔS), and stoichiometry of binding (n) are listed.