Formation of c 1 fragment ions in collision‐induced dissociation of glutamine‐containing peptide ions: a tip for de novo sequencing
peer-reviewed · Rapid Communications in Mass Spectrometry · 2004
| Date | 2004-09-30 |
| Type | peer-reviewed |
| Venue | Rapid Communications in Mass Spectrometry |
| Publisher | Wiley |
| Contribution | adjacent |
| DOI | 10.1002/rcm.1593 |
| Citations (OpenAlex) | 20 |
| Venue 2-year citedness | 1.80 |
Abstract
A c1 ion was observed with significant yield in the tandem mass (MS/MS) spectra of peptide ions containing glutamine as the second amino acid residue from the N-terminus. The c1 fragment was generated independently of the N-terminal residue of the peptide, but its abundance was strongly dependent on the side-chain identity. This ion is not a common fragmentation product in low-energy collision-induced dissociation of peptide ions, but it assists in identification of the first two amino acid residues, often difficult due to a low or absent signal from the heaviest y ion. A consecutive fragmentation mechanism is proposed, involving a b2 ion with a six-membered ring as an intermediate, to explain the exceptional stability of the c1 fragment ion. The utility of this information is discussed, especially in de novo sequencing of peptide ions.
Methods and tools
- c1 ions from Gln-containing peptides: Shows that peptides with glutamine at position two give an abundant c1 ion under low-energy CID, which helps assign the N-terminal two residues during de novo sequencing.