Evidence map›Paper›PMID 14512730›Full record

ArticleJournal of biomolecular NMR2003

Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.

Anja Böckmann, Adam Lange, Anne Galinier, Sorin Luca, Nicolas Giraud, Michel Juy, Henrike Heise, Roland Montserret, François Penin, Marc Baldus

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Atomic resolution structure of full-length human insulin fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. High-efficiency low-powerJournal of magnetic resonance (San Diego, Calif. : 1997) · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  12. Article
  13. Article
  14. Heteronuclear proton assisted recoupling.The Journal of chemical physics · 2011
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. NMR Determination of Protein pK(a) Values in the Solid State.The journal of physical chemistry letters · 2010
    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

10 authors.

Anja BöckmannInstitut de Biologie et Chimie des Protéines, C.N.R.S UMR 5086, 7, passage du Vercors, 69367 Lyon Cedex 07, France. a.bockmann@ibcp.fr
Adam Lange
Anne Galinier
Sorin Luca
Nicolas Giraud
Michel Juy
Henrike Heise
Roland Montserret
François Penin
Marc Baldus

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solid state NMR sample preparation and resonance assignments of the U-[13C,15N] 2x10.4 kDa dimeric form of the regulatory protein Crh in microcrystalline, PEG precipitated form are presented. Intra- and interresidue correlations using dipolar polarization transfer methods led to nearly complete sequential assignments of the protein, and to 88% of all 15N, 13C chemical shifts. For several residues, the resonance assignments differ significantly from those reported for the monomeric form analyzed by solution state NMR. Dihedral angles obtained from a TALOS-based statistical analysis suggest that the microcrystalline arrangement of Crh must be similar to the domain-swapped dimeric structure of a single crystal form recently solved using X-ray crystallography. For a limited number of protein residues, a remarkable doubling of the observed NMR resonances is observed indicative of local static or dynamic conformational disorder. Our study reports resonance assignments for the largest protein investigated by solid state NMR so far and describes the conformational dimeric variant of Crh with previously unknown chemical shifts.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsCrystallizationDimerizationModels, MolecularMolecular WeightNuclear Magnetic Resonance, BiomolecularPhosphoproteinsProtein ConformationSolutionsBacterial ProteinsCrh protein, Bacillus subtilisPhosphoproteinsSolutions

Identifiers

What OpenQuestion holds

Textmetadata
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.