Table 1.
Effect of Rnd3 Peptide Modifications on 14-3-3 Binding
| Rnd3 Peptide | Stoichiometry (N) | Kd (μM) | TΔS (kcal/mol) | ΔH (kcal/mol) | ΔG (kcal/mol) |
|---|---|---|---|---|---|
| +P+F | 0.83 ± 0.014 | 0.069 ± 0.025 | 6.843 ± 0.24 | −2.956 ± 0.06 | −9.798 ± 0.23 |
| +P-F | 0.89 ± 0.017 | 1.06 ± 0.04 | 2.469 ± 0.231 | −5.683 ± 0.204 | −8.152 ± 0.027 |
| −P+Fa | - | ND | no binding | - | - |
| −P-Fa | - | ND | no binding | - | - |
Thermodynamic parameters for Rnd3 C-terminal peptides and 14-3-3ζ-binding constants are shown; mean ± SD, n = 3. Titrations of +P+F and +P-F peptides binding to 14-3-3ζ were carried out at 25°C. ND, not detectable; P, phosphorylation on S240; F, farnesylation; see Table S3 for peptides.
a
Binding of −P+F and −P-F peptides to 14-3-3ζ was tested at 15°C and 25°C, where binding was not detected.