Evidence map›Paper›PMID 19254856›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2009

Determining the helical tilt of membrane peptides using electron paramagnetic resonance spectroscopy.

Justin P Newstadt, Daniel J Mayo, Johnson J Inbaraj, Nidhi Subbaraman, Gary A Lorigan

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  7. Review
  8. Review
  9. Article
  10. 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.

Justin P NewstadtDepartment of Chemistry and Biochemistry, Miami University of Ohio, Room 137, Hughes Laboratories, Oxford, OH 45056-1465, USA.
Daniel J Mayo
Johnson J Inbaraj
Nidhi Subbaraman
Gary A Lorigan

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

Theoretical calculations of hyperfine splitting values derived from the EPR spectra of TOAC spin-labeled rigid aligned alpha-helical membrane peptides reveal a unique periodic variation. In the absence of helical motion, a plot of the corresponding hyperfine splitting values as a function of residue number results in a sinusoidal curve that depends on the helical tilt angle that the peptide makes with respect to the magnetic field. Motion about the long helical axis reduces the amplitude of the curve and averages out the corresponding hyperfine splitting values. The corresponding spectra can be used to determine the director axis tilt angle from the TOAC spin label, which can be used to calculate the helical tilt angle due to the rigidity of the TOAC spin label. Additionally, this paper describes a method to experimentally determine this helical tilt angle from the hyperfine splitting values of three consecutive residues.

Indexed as

Protein Structure, SecondaryAlgorithmsElectron Spin Resonance SpectroscopyMembrane ProteinsPeptidesSpin LabelsMembrane ProteinsPeptidesSpin Labels

Identifiers

PMID19254856
PMCPMC2666113

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.