Evidence map›Paper›PMID 16848493›Full record

ArticleJournal of the American Chemical Society2006

Determining the topology of integral membrane peptides using EPR spectroscopy.

Johnson J Inbaraj, Thomas B Cardon, Mikhail Laryukhin, Stuart M Grosser, Gary A Lorigan

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  6. Article
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  12. Article
  13. Peptide-lipid interactions: experiments and applications.International journal of molecular sciences · 2013
    Article
  14. Review
  15. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  16. Review
  17. Article
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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

5 authors at 1 institution in 1 country.

Johnson J InbarajDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, USA.
Thomas B Cardon
Mikhail Laryukhin
Stuart M Grosser
Gary A Lorigan
Miami University · US

Funding

EPR and Solid-State NMR Studies of Integral Membrane ProteinsR01GM080542 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2007 to 2011
$1.6M
MAGNETIC RESONANCE STUDIES OF MEMBRANE PROTEINSR15GM060259 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2000 to 2000
$105k
NIGMS NIH HHS GM60259-01NIGMS NIH HHS R01 GM080542
6 · The paper itself

Abstract

This paper reports on the development of a new structural biology technique for determining the membrane topology of an integral membrane protein inserted into magnetically aligned phospholipid bilayers (bicelles) using EPR spectroscopy. The nitroxide spin probe, 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC), was attached to the pore-lining transmembrane domain (M2delta) of the nicotinic acetylcholine receptor (AChR) and incorporated into a bicelle. The corresponding EPR spectra revealed hyperfine splittings that were highly dependent on the macroscopic orientation of the bicelles with respect to the static magnetic field. The helical tilt of the peptide can be easily calculated using the hyperfine splittings gleaned from the orientational dependent EPR spectra. A helical tilt of 14 degrees was calculated for the M2delta peptide with respect to the bilayer normal of the membrane, which agrees well with previous 15N solid-state NMR studies. The helical tilt of the peptide was verified by simulating the corresponding EPR spectra using the standardized MOMD approach. This new method is advantageous because: (1) bicelle samples are easy to prepare, (2) the helical tilt can be directly calculated from the orientational-dependent hyperfine splitting in the EPR spectra, and (3) EPR spectroscopy is approximately 1000-fold more sensitive than 15N solid-state NMR spectroscopy; thus, the helical tilt of an integral membrane peptide can be determined with only 100 microg of peptide. The helical tilt can be determined more accurately by placing TOAC spin labels at several positions with this technique.

Indexed as

Amino Acid SequenceCell MembraneComputer SimulationElectron Spin Resonance SpectroscopyProtein ConformationReceptors, NicotinicSpin LabelsReceptors, NicotinicSpin Labels

Identifiers

PMID16848493
PMCPMC2533427
OpenAlexW2092225471

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.