Evidence map›Paper›PMID 12652122›Full record

ArticleJournal of biomolecular NMR2003

Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment.

Hans L J Wienk, Mitcheell M Martínez, Gary N Yalloway, Jürgen M Schmidt, Carlos Pérez, Heinz Rüterjans, Frank Löhr

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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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Hans L J WienkInstitut für Biophysikalische Chemie, JW Goethe-Universität, Marie-Curie-Str 9, D-60439 Frankfurt am Main, Germany.
Mitcheell M Martínez
Gary N Yalloway
Jürgen M Schmidt
Carlos Pérez
Heinz Rüterjans
Frank Löhr

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A quantitative J-correlation pulse sequence is described that allows simultaneous determination of one-bond and two-bond nitrogen-carbon coupling constants for protonated or deuterated proteins. Coupling constants are calculated from volume ratios between cross peaks and reference axial peaks observed in a single 3D spectrum. Accurate backbone (1)J(NC'), (1)J(NCalpha), and (2)J(NCalpha) coupling constants are obtained for the two [(15)N;(13)C]-labeled, medium-sized proteins flavodoxin and xylanase and for the [(2)H;(15)N;(13)C]-labeled, large protein DFPase. A dependence of one-bond and two-bond J(NCalpha) values on protein backbone psi torsion angles is readily apparent, in agreement with previously found correlations. In addition, the experiment is performed on isotropic as well as aligned protein to measure associated (15)N-(13)C residual dipolar couplings.

Indexed as

BacillusCarbonCarbon IsotopesCloning, MolecularDeuteriumEscherichia coliIsotope LabelingMagnetic Resonance SpectroscopyNitrogenProtein ConformationProteinsRecombinant ProteinsTritiumXylan Endo-1,3-beta-XylosidaseXylosidasesCarbonCarbon IsotopesDeuteriumNitrogenProteinsRecombinant ProteinsTritiumXylan Endo-1,3-beta-XylosidaseXylosidases

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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.