Evidence map›Paper›PMID 21806918›Full record

ArticleBiophysical journal2011

Site-specific solid-state NMR detection of hydrogen-deuterium exchange reveals conformational changes in a 7-helical transmembrane protein.

Shenlin Wang, Lichi Shi, Izuru Kawamura, Leonid S Brown, Vladimir Ladizhansky

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 40 citations in OpenAlex.

  1. A random fractionalMagnetic resonance letters · 2026
    Article
  2. Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
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  10. Probing membrane protein structure using water polarization transfer solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    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 2 institutions in 2 countries.

Shenlin WangDepartment of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.
Lichi Shi
Izuru Kawamura
Leonid S Brown
Vladimir Ladizhansky
University of Guelph · CAYokohama National University · JP

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific detection of light-induced hydrogen-deuterium exchange in the lipid-embedded heptahelical transmembrane photosensor Anabaena sensory rhodopsin to pinpoint the location of its conformational changes upon activation. We show that the light-induced conformational changes result in a dramatic, but localized, increase in the exchange in the transmembrane regions. Most notably, the cytoplasmic half of helix G and the cytoplasmic ends of helices B and C exchange more extensively, probably as a result of their relative displacement in the activated state, allowing water to penetrate into the core of the protein. These light-induced rearrangements must provide the structural basis for the photosensory function of Anabaena sensory rhodopsin.

Indexed as

Deuterium Exchange MeasurementNuclear Magnetic Resonance, BiomolecularAnabaenaBacterial ProteinsModels, MolecularProtein Structure, SecondaryRhodopsinBacterial ProteinsRhodopsin

Identifiers

PMID21806918
PMCPMC3145272
OpenAlexW1987120568

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.