Evidence map›Paper›PMID 24752819›Full record

ArticleJournal of biomolecular NMR2014

Sensitivity gains, linearity, and spectral reproducibility in nonuniformly sampled multidimensional MAS NMR spectra of high dynamic range.

Christopher L Suiter, Sivakumar Paramasivam, Guangjin Hou, Shangjin Sun, David Rice, Jeffrey C Hoch, David Rovnyak, Tatyana Polenova

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Cross polarization stability in multidimensional NMR spectroscopy of biological solids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024
    Article
  4. Article
  5. Article
  6. High fidelity sampling schedules for NMR spectra of high dynamic range.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Article
  7. Article
  8. Article
  9. Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  10. Article
  11. Review
  12. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  13. Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR.Angewandte Chemie (International ed. in English) · 2017
    Article
  14. GdJournal of biomolecular NMR · 2017
    Article
  15. Article
  16. Sensitivity of nonuniform sampling NMR.The journal of physical chemistry. B · 2015
    Article
  17. Article
  18. Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  19. MAS NMR of HIV-1 protein assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015
    Article
  20. 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

8 authors.

Christopher L SuiterDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA, csuiter@udel.edu.
Sivakumar Paramasivam
Guangjin Hou
Shangjin Sun
David Rice
Jeffrey C Hoch
David Rovnyak
Tatyana Polenova

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
COBRE on Membrane Protein Production and CharacterizationP30GM103519 · NIGMS · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2012 to 2014
$3.3M
THE ROLE OF MITOCHONDRIAL TRANSPORT PROTEINS IN HEPATOCYTES AND ADIPOCYTESP30RR031160 · NCRR · UNIVERSITY OF DELAWARE · PI POLENOVA, TATYANA · 2010 to 2011
$2.6M
Structure and Dynamics of CAP-GLY: Microtubule Assemblies by Solid-State NMRR01GM085306 · NIGMS · UNIVERSITY OF DELAWARE · PI POLENOVA, TATYANA, WILLIAMS, JOHN CHARLES · 2010 to 2014
$1.4M
NCRR NIH HHS P30 RR031160NCRR NIH HHS P30RR031160NIGMS NIH HHS P30 GM103519NIGMS NIH HHS P30GM103519NIGMS NIH HHS P50 GM082251NIGMS NIH HHS P50GM082251NIGMS NIH HHS R01 GM085306NIGMS NIH HHS R01GM085306
6 · The paper itself

Abstract

Recently, we have demonstrated that considerable inherent sensitivity gains are attained in MAS NMR spectra acquired by nonuniform sampling (NUS) and introduced maximum entropy interpolation (MINT) processing that assures the linearity of transformation between the time and frequency domains. In this report, we examine the utility of the NUS/MINT approach in multidimensional datasets possessing high dynamic range, such as homonuclear (13)C-(13)C correlation spectra. We demonstrate on model compounds and on 1-73-(U-(13)C,(15)N)/74-108-(U-(15)N) E. coli thioredoxin reassembly, that with appropriately constructed 50% NUS schedules inherent sensitivity gains of 1.7-2.1-fold are readily reached in such datasets. We show that both linearity and line width are retained under these experimental conditions throughout the entire dynamic range of the signals. Furthermore, we demonstrate that the reproducibility of the peak intensities is excellent in the NUS/MINT approach when experiments are repeated multiple times and identical experimental and processing conditions are employed. Finally, we discuss the principles for design and implementation of random exponentially biased NUS sampling schedules for homonuclear (13)C-(13)C MAS correlation experiments that yield high-quality artifact-free datasets.

Indexed as

Nuclear Magnetic Resonance, BiomolecularCarbon-13 Magnetic Resonance SpectroscopyDatabases, ProteinHistidinePeptidesReproducibility of ResultsThioredoxinsHistidinePeptidesThioredoxins

Identifiers

PMID24752819
PMCPMC4142058

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.