TABLE 3.
Characterization of HBx cysteine residues in Huh-7 cellsa
| Cysteine position(s)b | Sequencec | Peptide position(s)d | Confidence (%)e | MW (charge state)f |
|---|---|---|---|---|
| 6, 7 | LCCQLDPAR | 2, 3 | 98.89 | 1,131.516 (2) |
| 17, 26 | DVLCLRPVGAESCGRPFSGSLGTLSSPSPSAVPTDHGAHLSLR | 4, 13 | 99.00 | 4,444.202 (5) |
| 61, 69 | GLPVCAFSSAGPCALR | 5, 13 | 99.00 | 1,661.802 (2) |
| 115 | DCLFKDWEELGEEIR | 2 | 99.00 | 1,937.883 (3) |
| 137 | LKVFVLGGCR | 9 | 98.33 | 1,147.654 (3) |
| 143, 148 | LVCAPAPCNFFTSA | 3, 8 | 99.00 | 1,553.701 (2) |
a
Analysis performed by LC-MS.
b
Position(s) of the cysteine in the HBx protein sequence.
c
Cysteine residues are underlined.
d
Position(s) of the cysteine in the peptide sequence modified by iodoacetamide.
e
Confidence of identification evaluated by Protein Pilot.
f
MW, molecular weight of the peptide with the modification on cysteines. The charge state of the ion detected by mass spectrometry is in parentheses.