Evidence map›Paper›PMID 26800993›Full record

ArticleJournal of biomolecular NMR2016

Nitrogen-detected TROSY yields comparable sensitivity to proton-detected TROSY for non-deuterated, large proteins under physiological salt conditions.

Koh Takeuchi, Haribabu Arthanari, Misaki Imai, Gerhard Wagner, Ichio Shimada

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2016. 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. Journal of biomolecular NMR · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. More than Proton Detection-New Avenues for NMR Spectroscopy of RNA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  10. Review
  11. Article
  12. Article
  13. Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Review
  15. Evaluation ofJournal of biomolecular NMR · 2017
    Article
  16. Article
  17. A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation.Protein science : a publication of the Protein Society · 2016
    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

5 authors.

Koh TakeuchiMolecular Profiling Research Center for Drug Discovery, National Institute for Advanced Industrial Science and Technology, Tokyo, 135-0063, Japan.
Haribabu ArthanariDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA, 02115, USA.
Misaki ImaiResearch and Development Department, Japan Biological Informatics Consortium, Tokyo, 135-0063, Japan.
Gerhard WagnerDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA, 02115, USA. gerhard_wagner@hms.harvard.edu.
Ichio ShimadaMolecular Profiling Research Center for Drug Discovery, National Institute for Advanced Industrial Science and Technology, Tokyo, 135-0063, Japan. shimada@iw-nmr.f.u-tokyo.ac.jp.

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
STRUCTURE BASIS OF IMMUNE-CELL SURFACE RECEPTOR FUNCTIONR01AI037581 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2021
$6.7M
NIAID NIH HHS AI37581NIAID NIH HHS R01 AI037581NIBIB NIH HHS EB002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM047467NIGMS NIH HHS P01 GM047467
6 · The paper itself

Abstract

Direct detection of the TROSY component of proton-attached (15)N nuclei ((15)N-detected TROSY) yields high quality spectra with high field magnets, by taking advantage of the slow (15)N transverse relaxation. The slow transverse relaxation and narrow line width of the (15)N-detected TROSY resonances are expected to compensate for the inherently low (15)N sensitivity. However, the sensitivity of (15)N-detected TROSY in a previous report was one-order of magnitude lower than in the conventional (1)H-detected version. This could be due to the fact that the previous experiments were performed at low salt (0-50 mM), which is advantageous for (1)H-detected experiments. Here, we show that the sensitivity gap between (15)N and (1)H becomes marginal for a non-deuterated, large protein (τ c = 35 ns) at a physiological salt concentration (200 mM). This effect is due to the high salt tolerance of the (15)N-detected TROSY. Together with the previously reported benefits of the (15)N-detected TROSY, our results provide further support for the significance of this experiment for structural studies of macromolecules when using high field magnets near and above 1 GHz.

Indexed as

ProtonsCarrier ProteinsEscherichia coliEscherichia coli ProteinsNitrogenNuclear Magnetic Resonance, BiomolecularProtein PrecursorsCarrier ProteinsEscherichia coli ProteinsNitrogenpreMBP protein, E coliProtein PrecursorsProtonsHigh field magnetNitrogen detectionProtein NMRSalt concentrationSensitivityTROSY

Identifiers

PMID26800993
PMCPMC4871712

What OpenQuestion holds

Textmetadata
LicenceTDM
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.