Evidence map›Paper›PMID 25129622›Full record

ArticleJournal of biomolecular NMR2014

¹³Cα decoupling during direct observation of carbonyl resonances in solution NMR of isotopically enriched proteins.

Jinfa Ying, Fang Li, Jung Ho Lee, Ad Bax

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 26 citations in OpenAlex.

  1. Direct evidence for a deprotonated lysine serving as a H-bond "acceptor" in a photoreceptor protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. OptimalNature protocols · 2024
    Review
  3. Chemical reviews · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Visualizing unresolved scalar couplings by real-time J-upscaled NMR.Journal of the American Chemical Society · 2015
    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

4 authors at 2 institutions in 1 country.

Jinfa YingLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Fang Li
Jung Ho Lee
Ad Bax
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Methods to accelerate protein structure determination by solution NMRZIADK029046 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2009 to 2025
$12.8M
Structure and membrane binding of alpha-synucleinZIADK029047 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2009 to 2018
$5.6M
Intramural NIH HHS ZIA DK029046Intramural NIH HHS ZIA DK029047
6 · The paper itself

Abstract

Direct detection of (13)C can be advantageous when studying uniformly enriched proteins, in particular for paramagnetic proteins or when hydrogen exchange with solvent is fast. A scheme recently introduced for long-observation-window band-selective homonuclear decoupling in solid state NMR, LOW-BASHD (Struppe et al. in J Magn Reson 236:89-94, 2013) is shown to be effective for (13)C(α) decoupling during direct (13)C' observation in solution NMR experiments too. For this purpose, adjustment of the decoupling pulse parameters and delays is demonstrated to be important for increasing spectral resolution, to reduce three-spin effects, and to decrease the intensity of decoupling side-bands. LOW-BASHD then yields (13)C' line widths comparable to those obtained with the popular IPAP method, while enhancing sensitivity by ca 35 %. As a practical application of LOW-BASHD decoupling, requiring quantitative intensity measurement over a wide dynamic range, the impact of lipid binding on the (13)C'-detected NCO spectrum of the intrinsically disordered protein α-synuclein is compared with that on the (1)H-detected (1)H-(15)N HSQC spectrum. Results confirm that synuclein's "dark state" behavior is not caused by paramagnetic relaxation or rapid hydrogen exchange.

Indexed as

alpha-SynucleinCarbon IsotopesLipidsModels, ChemicalNuclear Magnetic Resonance, BiomolecularProteinsalpha-SynucleinCarbon IsotopesLipidsProteins

Identifiers

PMID25129622
PMCPMC4156133
OpenAlexW2028475635

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.