Evidence map›Paper›PMID 20518534›Full record

ArticleAnalytical chemistry2010

Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry.

Christine M Hebling, Christopher R Morgan, Darrel W Stafford, James W Jorgenson, Kasper D Rand, John R Engen

Abstract read
In one paragraph

Article in Analytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

78 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  5. Article
  6. Article
  7. MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS.Journal of the American Society for Mass Spectrometry · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
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  19. Article
  20. Review

18 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Christine M HeblingDepartment of Chemistry, Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
Christopher R Morgan
Darrel W Stafford
James W Jorgenson
Kasper D Rand
John R Engen
Northeastern University · USUniversity of North Carolina at Chapel Hill · US

Funding

STRUCTURE/FUNCTION OF THE GAMMA GLUTAMYL CARBOXYLASER01HL048318 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W · 1992 to 2011
$3.4M
Protein conformational change upon membrane associationR01GM086507 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2009 to 2012
$1.6M
NHLBI NIH HHS HL48318NHLBI NIH HHS R01 HL048318NIGMS NIH HHS GM086507NIGMS NIH HHS R01 GM086507
6 · The paper itself

Abstract

The study of membrane protein structure and enzymology has traditionally been hampered by the inherent insolubility of membrane proteins in aqueous environments and experimental challenges in emulating an in vivo lipid environment. Phospholipid bilayer nanodiscs have recently been shown to be of great use for the study of membrane proteins since they offer a controllable, stable, and monodisperse model membrane with a nativelike lipid bilayer. Here we report the integration of nanodiscs with hydrogen exchange (HX) mass spectrometry (MS) experiments, thereby allowing for analysis of the native conformation of membrane proteins. gamma-Glutamyl carboxylase (GGCX), an approximately 94 kDa transmembrane protein, was inserted into nanodiscs and labeled with deuterium oxide under native conditions. Analytical parameters including sample-handling and chromatographic separation were optimized to measure the incorporation of deuterium into GGCX. Coupling nanodisc technology with HX MS offers an effective approach for investigating the conformation and dynamics of membrane proteins in their native environment and is therefore capable of providing much needed insight into the function of membrane proteins.

Indexed as

Carbon-Carbon LigasesDeuterium Exchange MeasurementDeuterium OxideHydrogen-Ion ConcentrationLipid BilayersMass SpectrometryMembrane ProteinsNanostructuresPhospholipidsCarbon-Carbon LigasesDeuterium Oxideglutamyl carboxylaseLipid BilayersMembrane ProteinsPhospholipids

Identifiers

PMID20518534
PMCPMC2895417
OpenAlexW2048927314

What OpenQuestion holds

Textmetadata
LicenceTDM
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.