Evidence map›Paper›PMID 24360766›Full record

ReviewJournal of magnetic resonance (San Diego, Calif. : 1997)2014

Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins.

Jinfa Ying, Julien Roche, Ad Bax

Abstract readReview
In one paragraph

Review in Journal of magnetic resonance (San Diego, Calif. : 1997), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

31 citing papers in PubMed, 123 citations in OpenAlex.

  1. Deep Learning Assisted Proton Pure Shift NMR Spectroscopy.Journal of the American Chemical Society · 2026
    Article
  2. Article
  3. Article
  4. Neural net analysis of NMR spectra from strongly-coupled spin systems.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024
    Article
  5. Article
  6. Conformation Analysis and Stereodynamics of SymmetricallyMolecules (Basel, Switzerland) · 2024
    Article
  7. Solvent Suppression in Pure Shift NMR.Analytical chemistry · 2024
    Article
  8. Simultaneous Broadband Suppression of Homonuclear and Heteronuclear Couplings inChemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Dispersion from CJournal of biomolecular NMR · 2020
    Article
  13. Article
  14. Practical aspects of real-time pure shift HSQC experiments.Magnetic resonance in chemistry : MRC · 2018
    Article
  15. The GNAT: A new tool for processing NMR data.Magnetic resonance in chemistry : MRC · 2018
    Article
  16. Article
  17. Article
  18. Quarterly intrinsic disorder digest (April-May-June, 2014).Intrinsically disordered proteins · 2017
    Article
  19. Article
  20. 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

3 authors at 1 institution 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.
Julien RocheLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Ad BaxLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: bax@nih.gov.
National Institutes of Health · US

Funding

Protein structure and dynamics from residual dipolar couplingsZIADK029048 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2009 to 2018
$4.6M
Study of hemagglutinin membrane fusion domainZIADK069017 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, AD · 2009 to 2015
$1.9M
Intramural NIH HHS ZIA DK029048
6 · The paper itself

Abstract

Application of band-selective homonuclear (BASH) (1)H decoupling pulses during acquisition of the (1)H free induction decay is shown to be an efficient procedure for removal of scalar and residual dipolar couplings between amide and aliphatic protons. BASH decoupling can be applied in both dimensions of a homonuclear 2D NMR experiment and is particularly useful for enhancing spectral resolution in the H(N)-H(α) region of NOESY spectra of peptides and proteins, which contain important information on the backbone torsion angles. The method then also prevents generation of zero quantum and Hz(N)-Hz(α) terms, thereby facilitating analysis of intraresidue interactions. Application to the NOESY spectrum of a hexapeptide fragment of the intrinsically disordered protein α-synuclein highlights the considerable diffusion anisotropy present in linear peptides. Removal of residual dipolar couplings between H(N) and aliphatic protons in weakly aligned proteins increases resolution in the (1)H-(15)N HSQC region of the spectrum and allows measurement of RDCs in samples that are relatively strongly aligned. The approach is demonstrated for measurement of RDCs in protonated (15)N/(13)C-enriched ubiquitin, aligned in Pf1, yielding improved fitting to the ubiquitin structure.

Indexed as

AnimalsAnisotropyHumansLiquid CrystalsNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsProteinsDiffusion anisotropyIDPLiquid crystalNOESYRDCResidual dipolar couplingSynucleinUbiquitinWeak alignment

Identifiers

PMID24360766
PMCPMC3965638
OpenAlexW2162215237

What OpenQuestion holds

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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.