Evidence map›Paper›PMID 23180049›Full record

ArticleJournal of biomolecular NMR2012

Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra.

Peter Bellstedt, Christian Herbst, Sabine Häfner, Jörg Leppert, Matthias Görlach, Ramadurai Ramachandran

Abstract read
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Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. PHRONESIS: A One-Shot Approach for Sequential Assignment of Protein Resonances by Ultrafast MAS Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
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  5. Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017
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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

6 authors.

Peter BellstedtBiomolecular NMR spectroscopy, Leibniz Institute for Age Research, Fritz Lipmann Institute, Jena, Germany.
Christian Herbst
Sabine Häfner
Jörg Leppert
Matthias Görlach
Ramadurai Ramachandran

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have carried out chemical shift correlation experiments with symmetry-based mixing sequences at high MAS frequencies and examined different strategies to simultaneously acquire 3D correlation spectra that are commonly required in the structural studies of proteins. The potential of numerically optimised symmetry-based mixing sequences and the simultaneous recording of chemical shift correlation spectra such as: 3D NCAC and 3D NHH with dual receivers, 3D NC'C and 3D C'NCA with sequential (13)C acquisitions, 3D NHH and 3D NC'H with sequential (1)H acquisitions and 3D CANH and 3D C'NH with broadband (13)C-(15)N mixing are demonstrated using microcrystalline samples of the β1 immunoglobulin binding domain of protein G (GB1) and the chicken α-spectrin SH3 domain.

Indexed as

Carbon IsotopesFourier AnalysisNerve Tissue ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProteinsSpectrinsrc Homology DomainsCarbon IsotopesG-substrateNerve Tissue ProteinsNitrogen IsotopesProteinsSpectrin

Identifiers

What OpenQuestion holds

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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.