Evidence map›Paper›PMID 19121592›Full record

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

High-resolution 1H MAS RFDR NMR of biological membranes.

Darryl Aucoin, Devin Camenares, Xin Zhao, Jay Jung, Takeshi Sato, Steven O Smith

Open access · greenAbstract 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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

12 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021
    Article
  5. Fast Magic-Angle SpinningAngewandte Chemie (International ed. in English) · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 2 institutions in 2 countries.

Darryl AucoinDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Devin Camenares
Xin Zhao
Jay Jung
Takeshi Sato
Steven O Smith
Stony Brook University · USOsaka University · JP

Funding

Structure-function studies of single transmembrane helix receptorsR01GM046732 · NIGMS · YALE UNIVERSITY · PI SMITH, STEVEN OWEN · 1996 to 2011
$4.2M
NMR of basic-aromatic clustersR01GM069651 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI SMITH, STEVEN OWEN · 2004 to 2007
$1.0M
ROTATIONAL RESONANCE NMR STRUCTURAL STUDIES OF RECEPTORSR55GM046732 · NIGMS · YALE UNIVERSITY · PI SMITH, STEVEN OWEN · 1994 to 1994
–
600 MHZ SOLID STATE NMR SPECTROMETERS10RR013889 · NCRR · STATE UNIVERSITY NEW YORK STONY BROOK · PI SMITH, STEVEN OWEN · 1999 to 1999
–
NCRR NIH HHS S10 RR13889NIGMS NIH HHS GM-06965NIGMS NIH HHS GM-46732NIGMS NIH HHS R01 GM046732NIGMS NIH HHS R01 GM069651
6 · The paper itself

Abstract

The combination of magic angle spinning (MAS) with the high-resolution (1)H NOESY NMR experiment is an established method for measuring through-space (1)H...(1)H dipolar couplings in biological membranes. The segmental motion of the lipid acyl chains along with the overall rotational diffusion of the lipids provides sufficient motion to average the (1)H dipolar interaction to within the range where MAS can be effective. One drawback of the approach is the relatively long NOESY mixing times needed for relaxation processes to generate significant crosspeak intensity. In order to drive magnetization transfer more rapidly, we use solid-state radiofrequency driven dipolar recoupling (RFDR) pulses during the mixing time. We compare the (1)H MAS NOESY experiment with a (1)H MAS RFDR experiment on dimyristoylphosphocholine, a bilayer-forming lipid and show that the (1)H MAS RFDR experiment provides considerably faster magnetization exchange than the standard (1)H MAS NOESY experiment. We apply the method to model compounds containing basic and aromatic amino acids bound to membrane bilayers to illustrate the ability to locate the position of aromatic groups that have penetrated to below the level of the lipid headgroups.

Indexed as

AlgorithmsModels, ChemicalComputer SimulationLipid BilayersMagnetic Resonance SpectroscopyPhospholipidsProtonsLipid BilayersPhospholipidsProtons

Identifiers

PMID19121592
PMCPMC2802820
OpenAlexW2015243633

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.