Table 1.
Cross-linking characteristics of cysteine-substitution mutants
| Mutants | Cβ–Cβ distance, Å | Extent of cross-linking |
|---|---|---|
| Disulfide | ||
| D29C/R403C | 5.1 | Partial |
| L194C/L410C | 6.9 | Minimal |
| L194C/L422C | 7.0 | Minimal |
| I197C/L406C | 6.5 | Minimal |
| L198C/L198C | 7.9 | Minimal |
| I201C/I201C | 6.5 | Partial |
| K216C/T433C | 5.7 | Partial |
| I220C/L430C | 6.5 | Minimal |
| I223C/I426C | 5.7 | Minimal |
| T226C/L423C | 6.5 | Minimal |
| R230C/L249C | 5.9 | Complete |
| Q207C/Q207C | 17.8 | Complete |
| Sulfenamide | ||
| K216/T433C | 5.7 | Complete |
Cysteine-substitution mutants were scored for cross-linking in the presence of added oxidant, as observed by SDS/PAGE mobility.