Evidence map›Paper›PMID 27801801›Full record

ArticleMolecules (Basel, Switzerland)2016

Assessment of the Presence and Strength of H-Bonds by Means of Corrected NMR.

Steve Scheiner

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Solvation and Ion-Pairing Effects of Choline Acetate Electrolyte in Protic and Aprotic Solvents Studied by NMR Titrations.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Special Issue: Intramolecular Hydrogen Bonding 2017.Molecules (Basel, Switzerland) · 2017
    Article
  13. Article
  14. Review
  15. Article
  16. Review
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

1 author.

Steve ScheinerDepartment of Chemistry and Biochemistry, Utah State University, Logan, UT 84322-0300, USA. steve.scheiner@usu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The downfield shift of the NMR signal of the bridging proton in a H-bond (HB) is composed of two elements. The formation of the HB causes charge transfer and polarization that lead to a deshielding. A second factor is the mere presence of the proton-accepting group, whose electron density and response to an external magnetic field induce effects at the position of the bridging proton, exclusive of any H-bonding phenomenon. This second positional shielding must be subtracted from the full observed shift in order to assess the deshielding of the proton caused purely by HB formation. This concept is applied to a number of H-bonded systems, both intramolecular and intermolecular. When the positional shielding is removed, the remaining chemical shift is in much better coincidence with other measures of HB strength.

Indexed as

Models, ChemicalNuclear Magnetic Resonance, BiomolecularDipeptidesHydrogen BondingDipeptidesanti-electrostatic H-bondaromatic amino acidC5 dipeptideCH··O H-bondβ-sheet

Identifiers

PMID27801801
PMCPMC6274571

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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.