Evidence map›Paper›PMID 25495802›Full record

ArticleAnalytical chemistry2015

Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.

Antonio N Calabrese, Thomas G Watkinson, Peter J F Henderson, Sheena E Radford, Alison E Ashcroft

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Ion mobility-mass spectrometry reveals the role of peripheral myelin protein dimers in peripheral neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Interfacing Membrane Mimetics with Mass Spectrometry.Accounts of chemical research · 2016
    Article
  19. Skp is a multivalent chaperone of outer-membrane proteins.Nature structural & molecular biology · 2016
    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

5 authors at 2 institutions in 1 country.

Antonio N CalabreseSchool of Molecular and Cellular Biology and ‡School of Biomedical Sciences, Astbury Centre for Structural Molecular Biology, University of Leeds , Leeds, LS2 9JT, United Kingdom.
Thomas G Watkinson
Peter J F Henderson
Sheena E Radford
Alison E Ashcroft
Institute of Structural and Molecular Biology · GBUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E012558/1Biotechnology and Biological Sciences Research Council BB/K000659/1Biotechnology and Biological Sciences Research Council BB/K501827/1Biotechnology and Biological Sciences Research Council BB/M012573/1Wellcome Trust 094232/Z/10/Z
6 · The paper itself

Abstract

Noncovalent mass spectrometry (MS) is emerging as an invaluable technique to probe the structure, interactions, and dynamics of membrane proteins (MPs). However, maintaining native-like MP conformations in the gas phase using detergent solubilized proteins is often challenging and may limit structural analysis. Amphipols, such as the well characterized A8-35, are alternative reagents able to maintain the solubility of MPs in detergent-free solution. In this work, the ability of A8-35 to retain the structural integrity of MPs for interrogation by electrospray ionization-ion mobility spectrometry-mass spectrometry (ESI-IMS-MS) is compared systematically with the commonly used detergent dodecylmaltoside. MPs from the two major structural classes were selected for analysis, including two β-barrel outer MPs, PagP and OmpT (20.2 and 33.5 kDa, respectively), and two α-helical proteins, Mhp1 and GalP (54.6 and 51.7 kDa, respectively). Evaluation of the rotationally averaged collision cross sections of the observed ions revealed that the native structures of detergent solubilized MPs were not always retained in the gas phase, with both collapsed and unfolded species being detected. In contrast, ESI-IMS-MS analysis of the amphipol solubilized MPs studied resulted in charge state distributions consistent with less gas phase induced unfolding, and the presence of lowly charged ions which exhibit collision cross sections comparable with those calculated from high resolution structural data. The data demonstrate that A8-35 can be more effective than dodecylmaltoside at maintaining native MP structure and interactions in the gas phase, permitting noncovalent ESI-IMS-MS analysis of MPs from the two major structural classes, while gas phase dissociation from dodecylmaltoside micelles leads to significant gas phase unfolding, especially for the α-helical MPs studied.

Indexed as

MicellesGasesGlucosidesIonsMembrane ProteinsPolymersPropylaminesProtein ConformationSpectrometry, Mass, Electrospray Ionizationamphipol A8-35dodecyl maltosideGasesGlucosidesIonsMembrane ProteinsMicellesPolymersPropylamines

Identifiers

PMID25495802
PMCPMC4636139
OpenAlexW2143265556

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.