TABLE 1.
Thermodynamic properties of AR LBD binding of FXXLF and LXXLL peptides by isothermal titration calorimetry at 26°Ca
| Peptide | Kd (μM) | Ka (105 M−1) | ΔH (kcal/mol) | ΔS (cal/mol) | ΔG (kcal/mol) | N |
|---|---|---|---|---|---|---|
| ARA54-FXXLF | 0.9 ± 0.2 | 11.7 ± 1.5 | −8.7 ± 2.3 | −1.4 ± 7.3 | −8.3 ± 0.1 | 1.0 ± 0.3 |
| AR-NH2-FXXLF | 1.2 ± 0.2 | 8.4 ± 0.2 | −5.7 ± 1.2 | 7.9 ± 4.5 | −8.1 ± 0.1 | 1.1 ± 0.1 |
| TIF2-LXXLL-III | 6.0 ± 1.1 | 1.7 ± 0.3 | −1.8 ± 0 | 18.1 ± 0.5 | −7.2 ± 0.1 | 1.4 ± 0.2 |
a
Binding parameters were determined as described in Materials and Methods and the legend to Fig. 7 by titrating ARA54 FXXLF peptide residues 447 to 465, AR NH2-terminal FXXLF peptide residues 20 to 30, and TIF2 LXXLL-III peptide residues 738 to 755 with the AR LBD using isothermal titration calorimetry. N, number of peptide binding sites per LBD.