Table 1. Thermodynamic parameters for the binding of UP1 to wild-type SLII and structural mutants.
| SLII construct | Kd (nM) | n | ΔG° | ΔH° | -TΔS° |
|---|---|---|---|---|---|
| WT | |||||
| site 1 | 0.5 ± 0.1 | 0.7 ± 0.1 | -12.7 ± 0.1 | -38.3 ± 0.5 | 25.6 ± 0.6 |
| site 2 | 178.1 ± 22.7 | 1.5 ± 0.2 | -9.2 ± 0.1 | -17.6 ± 0.3 | 8.4 ± 0.4 |
| SLIIΔL ΔBL | 28.4 ± 2.0 | 0.87 ± 0.01 | -10.2 ± 0.1 | -28.2 ± 0.2 | 17.9 ± 0.2 |
| SLIIΔBL | 239.0 ± 9.0 | 0.95 ± 0.3 | -9.01 ± 0.2 | -30.22 ± 5.3 | 21.14 ± 5.5 |
| SLIIGNRA | 967.3 ± 159.2 | 1.10 ± 0.05 | -8.2 ± 0.04 | -56.5 ± 1.3 | 48.3 ± 1.3 |
| SLIICCC | 138.5 ± 14.8 | 1.4 ± 0.4 | -9.4 ± 0.1 | -35.9 ± 3.4 | 26.5 ± 3.5 |
a Measurements were made at 298K in 40 mM KCl and 5mM K2PHO4, pH 6.5; bThermodynamic parameters presented as avg +/− std taken from two replicates.