Evidence map›Paper›PMID 31894471›Full record

ArticleJournal of biomolecular NMR2020

Simultaneous recording of intra- and inter-residue linking experiments for backbone assignments in proteins at MAS frequencies higher than 60 kHz.

Kshama Sharma, P K Madhu, Vipin Agarwal, Kaustubh R Mote

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Article in Journal of biomolecular NMR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Homonuclear Simplified Preservation of Equivalent Pathways Spectroscopy.The journal of physical chemistry letters · 2024
    Article
  4. Article
  5. Simultaneous recoupling of chemical shift tensors of two nuclei by R-symmetry sequences.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  6. Review
  7. Article
  8. PHRONESIS: A One-Shot Approach for Sequential Assignment of Protein Resonances by Ultrafast MAS Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  9. Chemical reviews · 2022
    Review
  10. Article
  11. Transferred-Rotational-Echo Double Resonance.The journal of physical chemistry. A · 2021
    Article
  12. 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.

Kshama SharmaTIFR Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research Hyderabad, 36/P Gopanpally, Serlingampally Mandal, Rangareddy District, Hyderabad, 500107, India.
P K MadhuTIFR Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research Hyderabad, 36/P Gopanpally, Serlingampally Mandal, Rangareddy District, Hyderabad, 500107, India.
Vipin AgarwalTIFR Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research Hyderabad, 36/P Gopanpally, Serlingampally Mandal, Rangareddy District, Hyderabad, 500107, India. vipin@tifrh.res.in.
Kaustubh R MoteTIFR Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research Hyderabad, 36/P Gopanpally, Serlingampally Mandal, Rangareddy District, Hyderabad, 500107, India. krmote@tifrh.res.in.ORCID http://orcid.org/0000-0002-5151-3987

Funding

Department of Science and Technology, Government of India IFA/CH/150Science and Engineering Research Board (IN) ECR/2017/001450
6 · The paper itself

Abstract

Obtaining site-specific assignments for the NMR spectra of proteins in the solid state is a significant bottleneck in deciphering their biophysics. This is primarily due to the time-intensive nature of the experiments. Additionally, the low resolution in the [Formula: see text]-dimension requires multiple complementary experiments to be recorded to lift degeneracies in assignments. We present here an approach, gleaned from the techniques used in multiple-acquisition experiments, which allows the recording of forward and backward residue-linking experiments in a single experimental block. Spectra from six additional pathways are also recovered from the same experimental block, without increasing the probe duty cycle. These experiments give intra- and inter residue connectivities for the backbone [Formula: see text], [Formula: see text], [Formula: see text] and [Formula: see text] resonances and should alone be sufficient to assign these nuclei in proteins at MAS frequencies > 60 kHz. The validity of this approach is tested with experiments on a standard tripeptide N-formyl methionyl-leucine-phenylalanine (f-MLF) at a MAS frequency of 62.5 kHz, which is also used as a test-case for determining the sensitivity of each of the experiments. We expect this approach to have an immediate impact on the way assignments are obtained at MAS frequencies [Formula: see text].

Indexed as

Carbon IsotopesN-Formylmethionine Leucyl-PhenylalanineNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularCarbon-13Carbon IsotopesN-Formylmethionine Leucyl-PhenylalanineNitrogen-15Nitrogen IsotopesFast MASMagic-angle-spinning solid-state NMRMultiplexingProton detectionResidue linking

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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.