Evidence map›Paper›PMID 26369778›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.

Yu Sun, Siavash Vahidi, Modupeola A Sowole, Lars Konermann

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 57 citations in OpenAlex.

  1. Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023
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  11. Polymers for Traveling Wave Ion Mobility Spectrometry Calibration.Journal of the American Society for Mass Spectrometry · 2017
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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.

Yu SunDepartment of Chemistry, The University of Western Ontario, London, ON, N6A 5B7, Canada.
Siavash VahidiDepartment of Chemistry, The University of Western Ontario, London, ON, N6A 5B7, Canada.
Modupeola A SowoleDepartment of Chemistry, The University of Western Ontario, London, ON, N6A 5B7, Canada.
Lars KonermannDepartment of Chemistry, The University of Western Ontario, London, ON, N6A 5B7, Canada. konerman@uwo.ca.
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The question whether electrosprayed protein ions retain solution-like conformations continues to be a matter of debate. One way to address this issue involves comparisons of collision cross sections (Ω) measured by ion mobility spectrometry (IMS) with Ω values calculated for candidate structures. Many investigations in this area employ traveling wave IMS (TWIMS). It is often implied that nanoESI is more conducive for the retention of solution structure than regular ESI. Focusing on ubiquitin, cytochrome c, myoglobin, and hemoglobin, we demonstrate that Ω values and collisional unfolding profiles are virtually indistinguishable under both conditions. These findings suggest that gas-phase structures and ion internal energies are independent of the type of electrospray source. We also note that TWIMS calibration can be challenging because differences in the extent of collisional activation relative to drift tube reference data may lead to ambiguous peak assignments. It is demonstrated that this problem can be circumvented by employing collisionally heated calibrant ions. Overall, our data are consistent with the view that exposure of native proteins to electrospray conditions can generate kinetically trapped ions that retain solution-like structures on the millisecond time scale of TWIMS experiments. ᅟ

Indexed as

AnimalsCalibrationCattleGasesIonsProtein ConformationProteinsProtein UnfoldingSpectrometry, Mass, Electrospray IonizationGasesIonsProteinsCollision cross sectionElectrosprayGas phase ionProtein structureProtein unfolding

Identifiers

PMID26369778
OpenAlexW1956276313

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.