Evidence map›Paper›PMID 20334357›Full record

ArticleJournal of the American Chemical Society2010

Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.

Ronald Soong, Pieter E S Smith, Jiadi Xu, Kazutoshi Yamamoto, Sang-Choul Im, Lucy Waskell, Ayyalusamy Ramamoorthy

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

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  13. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  14. 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

7 authors.

Ronald SoongBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.
Pieter E S Smith
Jiadi Xu
Kazutoshi Yamamoto
Sang-Choul Im
Lucy Waskell
Ayyalusamy Ramamoorthy

Funding

Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
PARTICIPATION OF CYTOCHROME B5 IN ANESTHETIC METABOLISMR01GM035533 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WASKELL, LUCY A · 1985 to 2010
$2.7M
Purchase of a 500 MHz Solid State NMR SpectrometerS10RR023597 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2007 to 2007
$500k
NCRR NIH HHS RR023597NCRR NIH HHS S10 RR023597NIGMS NIH HHS GM035533NIGMS NIH HHS GM084018NIGMS NIH HHS R01 GM084018
6 · The paper itself

Abstract

Structural biology of membrane proteins has rapidly evolved into a new frontier of science. Although solving the structure of a membrane protein with atomic-level resolution is still a major challenge, separated local field (SLF) NMR spectroscopy has become an invaluable tool in obtaining structural images of membrane proteins under physiological conditions. Recent studies have demonstrated the use of rotating-frame SLF techniques to accurately measure strong heteronuclear dipolar couplings between directly bonded nuclei. However, in these experiments, all weak dipolar couplings are suppressed. On the other hand, weak heteronuclear dipolar couplings can be measured using laboratory-frame SLF experiments, but only at the expense of spectral resolution for strongly dipolar coupled spins. In the present study, we implemented two-dimensional proton-evolved local-field (2D PELF) pulse sequences using either composite zero cross-polarization (COMPOZER-CP) or windowless isotropic mixing (WIM) for magnetization transfer. These PELF sequences can be used for the measurement of a broad range of heteronuclear dipolar couplings, allowing for a complete mapping of protein dynamics in a lipid bilayer environment. Experimental results from magnetically aligned bicelles containing uniformly (15)N-labeled cytochrome b(5) are presented and theoretical analyses of the new PELF sequences are reported. Our results suggest that the PELF-based experimental approaches will have a profound impact on solid-state NMR spectroscopy of membrane proteins and other membrane-associated molecules in magnetically aligned bicelles.

Indexed as

ProtonsAmino Acid SequenceAnimalsCell MembraneCytochromes b5Electron TransportHemeMagneticsMolecular Dynamics SimulationMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProtein Structure, TertiaryRabbitsSolubilityCytochromes b5HemeProtonsWater

Identifiers

PMID20334357
PMCPMC2860266

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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.