Evidence map›Paper›PMID 21563228›Full record

ArticleProtein science : a publication of the Protein Society2011

Probing the structure of membrane proteins with electron spin echo envelope modulation spectroscopy.

Daniel Mayo, Andy Zhou, Indra Sahu, Robert McCarrick, Parker Walton, Adam Ring, Kaylee Troxel, Aaron Coey, Jaclyn Hawn, Abdul-Hamid Emwas and 1 more

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2011. 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
–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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Comparison of lipid dynamics and permeability in styrene-maleic acid and diisobutylene-maleic acid copolymer lipid nanodiscs by electron paramagnetic resonance spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  4. Review
  5. Utilization ofBiochimica et biophysica acta. Biomembranes · 2018
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  12. Review
  13. Article
  14. Article
  15. 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

11 authors.

Daniel MayoDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Andy Zhou
Indra Sahu
Robert McCarrick
Parker Walton
Adam Ring
Kaylee Troxel
Aaron Coey
Jaclyn Hawn
Abdul-Hamid Emwas
Gary A Lorigan

Funding

MAGNETIC RESONANCE STUDIES OF MEMBRANE PROTEINSR15GM060259 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2000 to 2000
$105k
NIGMS NIH HHS GM60259-01
6 · The paper itself

Abstract

A new approach has been developed to probe the structural properties of membrane peptides and proteins using the pulsed electron paramagnetic resonance technique of electron spin echo envelope modulation (ESEEM) spectroscopy and the α-helical M2δ subunit of the acetylcholine receptor incorporated into phospholipid bicelles. To demonstrate the practicality of this method, a cysteine-mutated nitroxide spin label (SL) is positioned 1, 2, 3, and 4 residues away from a fully deuterated Val side chain (denoted i + 1 to i + 4). The characteristic periodicity of the α-helical structure gives rise to a unique pattern in the ESEEM spectra. In the i + 1 and i + 2 samples, the ²H nuclei are too far away to be detected. However, with the 3.6 residue per turn pattern of an α-helix, the i + 3 and i + 4 samples reveal a strong signal from the ²H nuclei of the Val side chain. Modeling studies verify these data suggesting that the closest ²H-labeled Val to SL distance would in fact be expected in the i + 3 and i + 4 samples. This technique is very advantageous, because it provides pertinent qualitative structural information on an inherently difficult system like membrane proteins in a short period of time (minutes) with small amounts of protein (μg).

Indexed as

Amino Acid SequenceAnimalsElectron Spin Resonance SpectroscopyFish ProteinsMolecular Sequence DataProtein Structure, SecondaryReceptor, Muscarinic M2Spin LabelsTorpedoFish ProteinsReceptor, Muscarinic M2Spin Labels

Identifiers

PMID21563228
PMCPMC3149182

What OpenQuestion holds

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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.