Evidence map›Paper›PMID 22723345›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR.

Michael J Knight, Andrew J Pell, Ivano Bertini, Isabella C Felli, Leonardo Gonnelli, Roberta Pierattelli, Torsten Herrmann, Lyndon Emsley, Guido Pintacuda

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing 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

74 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Chemical reviews · 2022
    Review
  12. MgeLife · 2022
    Article
  13. Article
  14. Effects of Ionic Liquids on Metalloproteins.Molecules (Basel, Switzerland) · 2021
    Review
  15. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    Article
  16. Article
  17. Dipolar Order Parameters in Large Systems With Fast Spinning.Frontiers in molecular biosciences · 2021
    Article
  18. Structure of a Protein-RNA Complex by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2020
    Article
  19. Article
  20. Probing Reversible Guest Binding with HyperpolarizedMolecules (Basel, Switzerland) · 2020
    Review

14 more citing papers are in PubMed but not listed here.

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

9 authors.

Michael J KnightCentre de Résonance Magnétique Nucléaire à Très Hauts Champs, Unité Mixte de Recherche 5280 Centre National de la Recherche Scientifique/Ecole Normale Supérieure de Lyon, Université Claude Bernard Lyon 1, 5 rue de la Doua, 69100 Villeurbanne, France.
Andrew J Pell
Ivano Bertini
Isabella C Felli
Leonardo Gonnelli
Roberta Pierattelli
Torsten Herrmann
Lyndon Emsley
Guido Pintacuda

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We introduce a new approach to improve structural and dynamical determination of large metalloproteins using solid-state nuclear magnetic resonance (NMR) with (1)H detection under ultrafast magic angle spinning (MAS). The approach is based on the rapid and sensitive acquisition of an extensive set of (15)N and (13)C nuclear relaxation rates. The system on which we demonstrate these methods is the enzyme Cu, Zn superoxide dismutase (SOD), which coordinates a Cu ion available either in Cu(+) (diamagnetic) or Cu(2+) (paramagnetic) form. Paramagnetic relaxation enhancements are obtained from the difference in rates measured in the two forms and are employed as structural constraints for the determination of the protein structure. When added to (1)H-(1)H distance restraints, they are shown to yield a twofold improvement of the precision of the structure. Site-specific order parameters and timescales of motion are obtained by a gaussian axial fluctuation (GAF) analysis of the relaxation rates of the diamagnetic molecule, and interpreted in relation to backbone structure and metal binding. Timescales for motion are found to be in the range of the overall correlation time in solution, where internal motions characterized here would not be observable.

Indexed as

CarbonCatalysisCatalytic DomainCopperCrystallizationHydrogenMagnetic Resonance SpectroscopyMetalloproteinsModels, MolecularMolecular ConformationNitrogenNormal DistributionNuclear Magnetic Resonance, BiomolecularProtonsCarbonCopperHydrogenMetalloproteinsNitrogenProtons

Identifiers

PMID22723345
PMCPMC3396464

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.