Evidence map›Paper›PMID 16023362›Full record

ArticleJournal of the American Society for Mass Spectrometry2005

Multidimensional separations of ubiquitin conformers in the gas phase: relating ion cross sections to H/D exchange measurements.

Errol W Robinson, Evan R Williams

Abstract readEvaluation Study
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Lipopeptide-mediated inhibition of Aflatoxin biosynthesis inCurrent research in food science · 2026
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  12. Gas-phase protein conformation/multimer ion formation by electrospray ion mobility-mass spectrometry: bovine insulin and ubiquitin.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  13. Article
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  15. To What Extent is FAIMS Beneficial in the Analysis of Proteins?Journal of the American Society for Mass Spectrometry · 2016
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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

2 authors.

Errol W RobinsonDepartment of Chemistry, University of California at Berkeley, 94720, Berkeley, CA, USA.
Evan R WilliamsDepartment of Chemistry, University of California at Berkeley, 94720, Berkeley, CA, USA. williams@cchem.berkeley.edu.

Funding

Protein Conformation and Noncovalent InteractionsR01GM064712 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2002 to 2009
$2.0M
NIGMS NIH HHS R01 GM064712NIGMS NIH HHS R01-GM64712
6 · The paper itself

Abstract

Investigating gas-phase structures of protein ions can lead to an improved understanding of intramolecular forces that play an important role in protein folding. Both hydrogen/deuterium (H/D) exchange and ion mobility spectrometry provide insight into the structures and stabilities of different gas-phase conformers, but how best to relate the results from these two methods has been hotly debated. Here, high-field asymmetric waveform ion mobility spectrometry (FAIMS) is combined with Fourier-transform ion cyclotron resonance mass spectrometry (FT/ICR MS) and is used to directly relate ubiquitin ion cross sections and H/D exchange extents. Multiple conformers can be identified using both methods. For the 9+ charge state of ubiquitin, two conformers (or unresolved populations of conformers) that have cross sections differing by 10% are resolved by FAIMS, but only one conformer is apparent using H/D exchange at short times. For the 12+ charge state, two conformers (or conformer populations) have cross sections differing by <1%, yet H/D exchange of these conformers differ significantly (6 versus 25 exchanges). These and other results show that ubiquitin ion collisional cross sections and H/D exchange distributions are not strongly correlated and that factors other than surface accessibility appear to play a significant role in determining rates and extents of H/D exchange. Conformers that are not resolved by one method could be resolved by the other, indicating that these two methods are highly complementary and that more conformations can be resolved with this combination of methods than by either method alone.

Indexed as

Models, ChemicalModels, MolecularComputer SimulationDeuterium Exchange MeasurementGasesIonsPhase TransitionProtein FoldingProtein IsoformsSpectrometry, Mass, Electrospray IonizationSpectroscopy, Fourier Transform InfraredUbiquitinGasesIonsProtein IsoformsUbiquitin

Identifiers

PMID16023362
PMCPMC2735248

What OpenQuestion holds

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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.