Table 1.
Thermodynamic Data for the Binding of Q8 to MXA Peptides
| peptide | Kd (μM)a | ΔHa (kcal mol−1) | −TΔSb (kcal mol−1) |
|---|---|---|---|
| MFA | 0.14 (±0.01) | −20.1 (±0.1) | 10.6 (±0.1) |
| MYA | 0.25 (±0.01) | −18.2 (±0.2) | 9.3 (±0.1) |
| MLA | 0.72 (±0.09) | −15.8 (±2.6) | 7.4 (±2.5) |
| MKA | 2.6 (±0.3) | −13.7 (±0.5) | 6.0 (±0.6) |
| MAA | >100 |
a
Mean values measured from at least three ITC experiments at 300 K in 10 mM sodium phosphate, pH 7.0. Standard deviations are in parentheses.
b
Entropic contributions to the free energy of binding were calculated from the Kd and ΔH values, with error propagated from those of Kd and ΔH.