Evidence map›Paper›PMID 19651525›Full record

ArticleJournal of the American Society for Mass Spectrometry2009

Charge-separation reactions of doubly-protonated peptides: effect of peptide chain length.

Alex G Harrison

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Formation of y + 10 and y + 11 ions in the collision-induced dissociation of peptide ions.Journal of the American Society for Mass Spectrometry · 2012
    Article
  6. Article
  7. Effect of N-terminal glutamic acid and glutamine on fragmentation of peptide ions.Journal of the American Society for Mass Spectrometry · 2010
    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

1 author.

Alex G HarrisonDepartment of Chemistry, University of Toronto, Toronto, Ontario, Canada. aharriso@chem.utoronto.ca

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The collision induced dissociation of doubly-protonated (Ala)(x)His (x = 5, 6, 7, 8, 10) peptides have been studied. The major fragmentation reactions observed are symmetrical amide bond cleavages to give the complementary b(m) and y(N-m) ions, where N is the total number of residues in the peptide. Minor asymmetric cleavage to give doubly-protonated y ions also is observed, involving cleavage near the N-terminus. The shorter peptides (x = 5, 6, 7) show major cleavage of the second amide bond to yield b2 and y(N-2) ions, while (Ala)10His shows major symmetrical cleavage at the fourth and fifth amide bonds. (Ala)8His appears to be a transitional peptide in showing substantial symmetrical cleavage at the second, fourth, and fifth amide bonds. The results are in general agreement with the bifurcating nature of charge separation noted by Zubarev (J. Am. Soc. Mass Spectrom.2008, 19, 1755-1763) from a statistical analysis of a large body of doubly-protonated tryptic peptide CID mass spectra. It is shown that the b2 ion derived from doubly-protonated (Ala)5His has a protonated oxazolone structure.

Indexed as

Models, ChemicalAlanineHistidineMass SpectrometryOligopeptidesProtein ConformationProtonsAlanineHistidineOligopeptidesProtons

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.