Evidence map›Paper›PMID 28864905›Full record

ArticleJournal of biomolecular NMR2017

Measurement of protein backbone

Maxim Mayzel, Alexandra Ahlner, Patrik Lundström, Vladislav Y Orekhov

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
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

9 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020
    Article
  7. Article
  8. Boosting the resolution of low-fieldJournal of biomolecular NMR · 2020
    Article
  9. 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

4 authors at 2 institutions in 1 country.

Maxim MayzelThe Swedish NMR Centre, University of Gothenburg, Box 465, 40530, Göteborg, Sweden.
Alexandra AhlnerDivision of Chemistry, Department of Physics, Chemistry and Biology, Linköping University, 58183, Linköping, Sweden.
Patrik LundströmDivision of Chemistry, Department of Physics, Chemistry and Biology, Linköping University, 58183, Linköping, Sweden.
Vladislav Y OrekhovThe Swedish NMR Centre, University of Gothenburg, Box 465, 40530, Göteborg, Sweden. vladislav.orekhov@nmr.gu.se.ORCID http://orcid.org/0000-0002-7892-6896
Linköping University · SEUniversity of Gothenburg · SE

Funding

Vetenskapsrådet 2015-04614
6 · The paper itself

Abstract

Peak overlap in crowded regions of two-dimensional spectra prevents characterization of dynamics for many sites of interest in globular and intrinsically disordered proteins. We present new three-dimensional pulse sequences for measurement of Carr-Purcell-Meiboom-Gill relaxation dispersions at backbone nitrogen and carbonyl positions. To alleviate increase in the measurement time associated with the additional spectral dimension, we use non-uniform sampling in combination with two distinct methods of spectrum reconstruction: compressed sensing and co-processing with multi-dimensional decomposition. The new methodology was validated using disordered protein CD79A from B-cell receptor and an SH3 domain from Abp1p in exchange between its free form and bound to a peptide from the protein Ark1p. We show that, while providing much better resolution, the 3D NUS experiments give the similar accuracy and precision of the dynamic parameters to ones obtained using traditional 2D experiments. Furthermore, we show that jackknife resampling of the spectra yields robust estimates of peak intensities errors, eliminating the need for recording duplicate data points.

Indexed as

Carbon IsotopesIntrinsically Disordered ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProteinsCarbon IsotopesIntrinsically Disordered ProteinsNitrogen-15Nitrogen IsotopesProteinsConformational exchangeDynamicsIDPNMRNUSTarget acquisition

Identifiers

PMID28864905
PMCPMC5626786
OpenAlexW418606678

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.