ArticleJournal of the American Society for Mass Spectrometry2011
A systematic study of acidic peptides for b-type sequence scrambling.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Combinatorial Labeling Method for Improving Peptide Fragmentation in Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity.Journal of the American Society for Mass Spectrometry · 2014Article
- Mass spectrometric strategies to improve the identification of Pt(II)-modification sites on peptides and proteins.Journal of the American Society for Mass Spectrometry · 2014Article
- Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.Analytical chemistry · 2014Article
- Non-direct sequence ions in the tandem mass spectrometry of protonated peptide amides--an energy-resolved study.Journal of the American Society for Mass Spectrometry · 2013Article
- Fragmentation reactions of methionine-containing protonated octapeptides and fragment ions therefrom: an energy-resolved study.Journal of the American Society for Mass Spectrometry · 2013Article
- Protonated dipeptide losses from b(5) and b(4) ions of side chain hydroxyl group containing pentapeptides.Journal of the American Society for Mass Spectrometry · 2013Article
- Investigation of scrambled ions in tandem mass spectra. Part 1. Statistical characterization.Journal of the American Society for Mass Spectrometry · 2012Article
- Formation of y + 10 and y + 11 ions in the collision-induced dissociation of peptide ions.Journal of the American Society for Mass Spectrometry · 2012Article
- Fragmentation reactions of b(5) and a (5) ions containing proline--the structures of a(5) ions.Journal of the American Society for Mass Spectrometry · 2012Article
- Occurrence of C-terminal residue exclusion in peptide fragmentation by ESI and MALDI tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A systematic study was carried out to examine the effects of acidic amino acid residues and the position of the acidic group on the cyclization of b ions. The study utilized the model C-terminal amidated peptides XAAAAAA, AXAAAAA, AAXAAAA, AAAXAAA, AAAAXAA, AAAAAXA, AAAAAAX, XXAAAAAA, AAXXAAAA, AAAAXXAA, and AAAAAAXX, where X is a glutamic acid (E) or aspartic acid (D) residue. The CID mass spectra of b (n) (where n=7 and 8) ions derived from XAAAAAA, AAAXAAA, AAAAAAX and XXAAAAAA, AAXXAAAA, AAAAXXAA, and AAAAAAXX exhibited very similar fragmentation patterns for both the glutamic and the aspartic acid peptide series. The CID mass spectra of MH(+) derived from model peptides presented substantial direct and non-direct sequence b ions. The results indicate that b ions produced from acidic peptides can also undergo head-to-tail cyclization, which is the reason for the formation of the non-direct sequence b ions. The b ion spectra derived from the peptides became more complex as the number of acidic residues in the peptides increased. Side chains of glutamic and aspartic acid did not inhibit the cyclization of the b ions. Substantial water elimination was observed in all CID spectra of b (7) and b (8) ions. Finally, the preferential cleavage of glutamic or aspartic acid residues from macrocyclic structures of b ions was also investigated under various collision energy conditions.
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