Evidence map›Paper›PMID 17235497›Full record

ArticleJournal of biomolecular NMR2007

J-Spectroscopy in the presence of residual dipolar couplings: determination of one-bond coupling constants and scalable resolution.

Julien Furrer, Michael John, Horst Kessler, Burkhard Luy

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2007. 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
–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

7 citing papers in PubMed.

  1. LowCOST-HSQC Variants for Fast-Pulsing High ωMagnetic resonance in chemistry : MRC · 2026
    Article
  2. Robust bilinear rotations II.Magnetic resonance (Gottingen, Germany) · 2026
    Article
  3. Dual bilinear rotations.Magnetic resonance (Gottingen, Germany) · 2026
    Article
  4. Robust bilinear rotations.Science advances · 2025
    Article
  5. Article
  6. Article
  7. 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.

Julien FurrerOrganisch-Chemisches Institut, Universität Heidelberg, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.
Michael John
Horst Kessler
Burkhard Luy

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The access to weak alignment media has fuelled the development of methods for efficiently and accurately measuring residual dipolar couplings (RDCs) in NMR-spectroscopy. Among the wealth of approaches for determining one-bond scalar and RDC constants only J-modulated and J-evolved techniques retain maximum resolution in the presence of differential relaxation. In this article, a number of J-evolved experiments are examined with respect to the achievable minimum linewidth in the J-dimension, using the peptide PA4 and the 80-amino-acid-protein Saposin C as model systems. With the JE-N-BIRDd,X-HSQC experiment, the average full-width at half height could be reduced to approximately 5 Hz for the protein, which allows the additional resolution of otherwise unresolved peaks by the active (J+D)-coupling. Since RDCs generally can be scaled by the choice of alignment medium and alignment strength, the technique introduced here provides an effective resort in cases when chemical shift differences alone are insufficient for discriminating signals. In favorable cases even secondary structure elements can be distinguished.

Indexed as

Magnetic Resonance SpectroscopyModels, ChemicalModels, MolecularMolecular ConformationNitrogen IsotopesPeptidesProtonsSaposinsSoftwareSpectrophotometryTemperatureNitrogen IsotopesPeptidesProtonsSaposins

Identifiers

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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.