Evidence map›Paper›PMID 12018482›Full record

ArticleJournal of biomolecular NMR2002

Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.

Karin Kloiber, Wolfgang Schüler, Robert Konrat

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Using Cross-Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  3. Article
  4. Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019
    Review
  5. Article
  6. NMR contributions to structural dynamics studies of intrinsically disordered proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Review
  7. Article
  8. Article
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  14. Article
  15. Article
  16. Article
  17. Chemical shift-based methods in NMR structure determination.Progress in nuclear magnetic resonance spectroscopy
    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

3 authors.

Karin KloiberInstitute of Organic Chemistry, University of Innsbruck, Austria.
Wolfgang Schüler
Robert Konrat

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The simultaneous interpretation of a suite of dipole-dipole and dipole-CSA cross-correlation rates involving the backbone nuclei 13Calpha, 1Halpha, 13CO, 15N and 1HN can be used to resolve the ambiguities associated with each individual cross-correlation rate. The method is based on the transformation of experimental cross-correlation rates via calculated values based on standard peptide plane geometry and solid-state 13CO CSA parameters into a dihedral angle probability surface. Triple resonance NMR experiments with improved sensitivity have been devised for the quantification of relaxation interference between 1Halpha(i)-13Calpha(i)/15N(i)-1HN(i) and 1Halpha(i-1)-13Calpha(i-1)/15N(i)-1HN(i) dipole-dipole mechanisms in 15N, 13C-labeled proteins. The approach is illustrated with an application to 13C, 15N-labeled ubiquitin.

Indexed as

Carbon IsotopesNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProteinsStatistics as TopicUbiquitinCarbon IsotopesNitrogen IsotopesProteinsUbiquitin

Identifiers

What OpenQuestion holds

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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.