Evidence map›Paper›PMID 20541953›Full record

ArticleJournal of the American Society for Mass Spectrometry2010

Effect of the His residue on the cyclization of b ions.

Benjamin J Bythell, Michaela Knapp-Mohammady, Béla Paizs, Alex G Harrison

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Article
  2. Fragmentation Pathways of Lithiated Hexose Monosaccharides.Journal of the American Society for Mass Spectrometry · 2018
    Article
  3. Participation of C-H Protons in the Dissociation of a Proton Deficient Dipeptide.Journal of the American Society for Mass Spectrometry · 2017
    Article
  4. DNA Oligonucleotide Fragment Ion Rearrangements Upon Collision-Induced Dissociation.Journal of the American Society for Mass Spectrometry · 2015
    Article
  5. Article
  6. Article
  7. Article
  8. Evidence for sequence scrambling in collision-induced dissociation of y-type fragment ions.Journal of the American Society for Mass Spectrometry · 2013
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Conformation-specific spectroscopy of peptide fragment ions in a low-temperature ion trap.Journal of the American Society for Mass Spectrometry · 2012
    Article
  15. Article
  16. Article
  17. Relative stability of peptide sequence ions generated by tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Benjamin J BythellComputational Proteomics Group, German Cancer Research Center (DKFZ), Heidelberg, Germany.
Michaela Knapp-Mohammady
Béla Paizs
Alex G Harrison

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The MS(n) spectra of the [M + H](+) and b(5) peaks derived from the peptides HAAAAA, AHAAAA, AAHAAA, AAAHAA, and AAAAHA have been measured, as have the spectra of the b(4) ions derived from the first four peptides. The MS(2) spectra of the [M + H](+) ions show a substantial series of b(n) ions with enhanced cleavage at the amide bond C-terminal to His and substantial cleavage at the amide bond N-terminal to His (when there are at least two residues N-terminal to the His residue). There is compelling experimental and theoretical evidence for formation of nondirect sequence ions via cyclization/reopening chemistry in the CID spectra of the b ions when the His residue is near the C-terminus. The experimental evidence is less clear for ions when the His residue is near the N-terminus, although this may be due to the use of multiple alanine residues in the peptide making identifying scrambled peaks more difficult. The product ion mass spectra of the b(4) and b(5) ions from these isomeric peptides with cyclically permuted amino acid sequences are similar, but also show clear differences. This indicates less active cyclization/reopening followed by fragmentation of common structures for b(n) ions containing His than for sequences of solely aliphatic residues. Despite more energetically favorable cyclization barriers for the b(5) structures, the b(4) ions experimental data show more clear evidence of cyclization and sequence scrambling before fragmentation. For both b(4) and b(5) the energetically most favored structure is a macrocyclic isomer protonated at the His side chain.

Indexed as

CyclizationHistidineIonsIsomerismPeptidesTandem Mass SpectrometryThermodynamicsHistidineIonsPeptides

Identifiers

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.