Table 4.
Effects of urea on Mj-MAT activity.
| Protein | Urea unfoldinga | |
|---|---|---|
| D150% (M) | D250% (M) | |
| Wild typeb | 2.01 ± 0.13b | 5.79 ± 0.07b |
| W387F | 2.39 ± 0.18 | 6.20 ± 0.09 |
| W387F-Y49W | 1.85 ± 0.21 | 4.55 ± 0.12 |
| W387F-Y72W | 2.33 ± 0.19 | 5.70 ± 0.08 |
| W387F-Y85W | 1.86 ± 0.14 | 5.34 ± 0.11 |
| W387F-Y120W | 2.57 ± 0.16 | 5.73 ± 0.08 |
| W387F-Y170W | 1.90 ± 0.16 | 4.51 ± 0.08 |
| W387F-Y226W | 2.87 ± 0.17 | 5.92 ± 0.11 |
| W387F-Y233W | 1.61 ± 0.23 | 3.77 ± 0.09 |
| W387F-Y255W | 2.63 ± 0.17 | 5.83 ± 0.13 |
| W387F-Y267W | 1.62 ± 0.12 | 5.76 ± 0.06 |
| W387F-Y273W | 2.19 ± 0.12 | 5.43 ± 0.10 |
| W387F-Y323W | 2.24 ± 0.12 | 5.79 ± 0.15 |
| W387F-Y344W | 1.67 ± 0.11 | 3.53 ± 0.13 |
| W387F-Y371W | 1.15 ± 0.15 | 5.54 ± 0.06 |
a
Data were fit to the presence of two- or three states to obtain the characteristic denaturant concentrations at midpoint for each transition. The results shown are the mean ± SD of a typical experiment carried out in triplicate at 50 μg/ml protein concentration.
b
Data from table 2