Evidence map›Paper›PMID 23836693›Full record

ReviewChemphyschem : a European journal of chemical physics and physical chemistry2013

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes.

Henry G Hocking, Klaus Zangger, Tobias Madl

Abstract readReview
In one paragraph

Review in Chemphyschem : a European journal of chemical physics and physical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Review
  3. AcceleratedMagnetic resonance (Gottingen, Germany) · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Incorporation of DThe journal of physical chemistry. B · 2022
    Article
  8. Review
  9. NMR spectroscopy charges into protein surface electrostatics.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Review
  11. Metal-Chelated Polymer Nanodiscs for NMR Studies.Angewandte Chemie (International ed. in English) · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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.

Henry G HockingChair of Biomolecular NMR, Department Chemie, Technische Universität München, 85747 Garching (Germany); Institute of Structural Biology, Helmholtz Zentrum München, 85764 Neuherberg (Germany).
Klaus Zangger
Tobias Madl

Funding

Austrian Science Fund FWF P 25880
6 · The paper itself

Abstract

Characterisation of the structure and dynamics of large biomolecules and biomolecular complexes by NMR spectroscopy is hampered by increasing overlap and severe broadening of NMR signals. As a consequence, the number of available NMR spectroscopy data is often sparse and new approaches to provide complementary NMR spectroscopy data are needed. Paramagnetic relaxation enhancements (PREs) obtained from inert and soluble paramagnetic probes (solvent PREs) provide detailed quantitative information about the solvent accessibility of NMR-active nuclei. Solvent PREs can be easily measured without modification of the biomolecule; are sensitive to molecular structure and dynamics; and are therefore becoming increasingly powerful for the study of biomolecules, such as proteins, nucleic acids, ligands and their complexes in solution. In this Minireview, we give an overview of the available solvent PRE probes and discuss their applications for structural and dynamic characterisation of biomolecules and biomolecular complexes.

Indexed as

Coordination ComplexesMagneticsMolecular ProbesChelating AgentsGadoliniumModels, MolecularNuclear Magnetic Resonance, BiomolecularNucleic AcidsProteinsSolubilityChelating AgentsCoordination ComplexesGadoliniumMolecular ProbesNucleic AcidsProteinsmagnetic propertiesNMR spectroscopyproteinssolvent effectsstructural biology

Identifiers

PMID23836693
PMCPMC4171756

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.