Table 1.
Thermodynamic parameters of unfolding of native and chimeric class μ glutathione transferases
| Fluorescencea | CDb | |||||
| Transition 1 | Transition 2 | |||||
| Protein | ΔG(H2O)1 (kcal • mol−1) | m1 (kcal • mol−1 • M1) | ΔG(H2O)2 (kcal • mol−1) | m2 (kcal • mol−1 • M1) | ΔG(H2O) (kcal • mol−1) | m (kcal • mol−1 • M1) |
| M1–1c | 10.8 ± 1.8 | 1.0 ± 0.2 | 16.5 ± 0.1 | 3.5 ± 0.3 | 19.6 ± 0.2 | 3.38 ± 0.02 |
| M2–2c | 12.4 ± 0.9 | 1.8 ± 0.1 | 14.8 ± 0.8 | 3.1 ± 1.1 | 17.1 ± 1.1 | 3.7 ± 0.03 |
| M12–12 | 11.7 ± 0.8 | 1.0 ± 0.2 | 14.2 ± 1.9 | 3.1 ± 0.3 | 16.5 ± 0.4 | 3.5 ± 0.1 |
| M21–21 | 10.2 ± 0.8 | 0.8 ± 0.2 | 11.8 ± 1.4 | 2.5 ± 0.2 | 9.9 ± 0.3 | 1.99 ± 0.05 |
a Fluorescence data were fitted to a three-state unfolding mechanism (N2 ↔ 2I ↔ 2U).
b The CD data were fit to a two-state mechanism.
c Data for the native enzymes are from Hornby et al. (2000).