Table 2. Peptide fragments with dhA modifications in cysteine sites detected by mass spectrometry analyses.
| Mutant variant | Peptide sequence | Aminoacid range | Confidence (%) |
|---|---|---|---|
| R116C/T270C | TFELCSKSIESFEHR | 112–126 | 99 |
| R116C/T270C/G818C | DYKDDDDKSCLIPENLRNPK | 2–13 | 99 |
| R116C/T270C/G818C | TFELCSKSIESFEHR | 112–126 | 99 |
| R116C/T270C/G818C | VYDASSLLNEENGNTCFSTK | 255–274 | 97.2 |
Cysteines involved in disulphide bonds formation are marked in bold face.