Evidence map›Paper›PMID 22528205›Full record

ArticleJournal of the American Society for Mass Spectrometry2012

Conformational distribution of bradykinin [bk + 2 H]2+ revealed by cold ion spectroscopy coupled with FAIMS.

Georgios Papadopoulos, Annette Svendsen, Oleg V Boyarkin, Thomas R Rizzo

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.7field-weighted citation impact, top 4% of its field
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

17 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Cryogenic Vibrational Spectroscopy Provides Unique Fingerprints for Glycan Identification.Journal of the American Society for Mass Spectrometry · 2017
    Article
  7. Review
  8. Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016
    Article
  9. Gated Trapped Ion Mobility Spectrometry Coupled to Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016
    Article
  10. Article
  11. To What Extent is FAIMS Beneficial in the Analysis of Proteins?Journal of the American Society for Mass Spectrometry · 2016
    Article
  12. Article
  13. Infrared Spectroscopy of Mobility-Selected H+-Gly-Pro-Gly-Gly (GPGG).Journal of the American Society for Mass Spectrometry · 2015
    Article
  14. Fundamentals of trapped ion mobility spectrometry.Journal of the American Society for Mass Spectrometry · 2015
    Article
  15. Solution dependence of the collisional activation of ubiquitin [M + 7H](7+) ions.Journal of the American Society for Mass Spectrometry · 2014
    Article
  16. Article
  17. 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 at 1 institution in 1 country.

Georgios PapadopoulosLaboratoire de Chimie Physique Moléculaire, École Polytechnique Fédérale de Lausanne, CH-1015, Lausanne, Switzerland.
Annette Svendsen
Oleg V Boyarkin
Thomas R Rizzo
École Polytechnique Fédérale de Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We employ cold ion spectroscopy (CIS) in conjunction with high-field asymmetric waveform ion mobility spectrometry (FAIMS) to study the peptide bradykinin in its doubly protonated charge state ([bk + 2 H](2+)). Using FAIMS, we partially separate the electrosprayed [bk + 2 H](2+) ions into two conformational families and selectively introduce one of them at a time into a cold ion trap mass spectrometer, where we probe them by UV photofragment spectroscopy. Although the two conformational families have distinct electronic spectra, some cross-conformer contamination can be observed under certain conditions. We demonstrate that this contamination comes from isomerization of ions energized during and/or after their separation and not from incomplete separation of the initially electrosprayed conformations in the FAIMS stage. By varying the injection voltage of the ions into our mass spectrometer, we can intentionally induce isomerization to produce what seems to be a gas phase equilibrium distribution of conformers. This distribution is different from the one produced initially by electrospray, indicating that some of the conformers are kinetically trapped and may be related to conformers that are more favored in solution.

Indexed as

BradykininCold TemperatureIonsPhotochemical ProcessesProtein ConformationProtonsTandem Mass SpectrometryBradykininIonsProtons

Identifiers

PMID22528205
OpenAlexW1975325031

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.