Evidence map›Paper›PMID 26497830›Full record

ArticleJournal of biomolecular NMR2015

Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR.

Koh Takeuchi, Haribabu Arthanari, Ichio Shimada, Gerhard Wagner

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Identifying interactions between TDP-43's N-terminal and RNA-binding domains.Protein science : a publication of the Protein Society · 2025
    Article
  2. Selective [9-Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Journal of biomolecular NMR · 2025
    Article
  4. Hydrostatic Pressure Sensing by WNK kinases.Molecular biology of the cell · 2023
    Article
  5. Article
  6. Article
  7. Protein in-cell NMR spectroscopy at 1.2 GHz.Journal of biomolecular NMR · 2021
    Article
  8. Applications of Solution NMR in Drug Discovery.Molecules (Basel, Switzerland) · 2021
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. More than Proton Detection-New Avenues for NMR Spectroscopy of RNA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

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.
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.
Gerhard WagnerDepartment of Biochemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA, 02115, USA. gerhard_wagner@hms.harvard.edu.
Harvard University · USNational Institute of Advanced Industrial Science and Technology · 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

Detection of (15)N in multidimensional NMR experiments of proteins has sparsely been utilized because of the low gyromagnetic ratio (γ) of nitrogen and the presumed low sensitivity of such experiments. Here we show that selecting the TROSY components of proton-attached (15)N nuclei (TROSY (15)NH) yields high quality spectra in high field magnets (>600 MHz) by taking advantage of the slow (15)N transverse relaxation and compensating for the inherently low (15)N sensitivity. The (15)N TROSY transverse relaxation rates increase modestly with molecular weight but the TROSY gain in peak heights depends strongly on the magnetic field strength. Theoretical simulations predict that the narrowest line width for the TROSY (15)NH component can be obtained at 900 MHz, but sensitivity reaches its maximum around 1.2 GHz. Based on these considerations, a (15)N-detected 2D (1)H-(15)N TROSY-HSQC ((15)N-detected TROSY-HSQC) experiment was developed and high-quality 2D spectra were recorded at 800 MHz in 2 h for 1 mM maltose-binding protein at 278 K (τc ~ 40 ns). Unlike for (1)H detected TROSY, deuteration is not mandatory to benefit (15)N detected TROSY due to reduced dipolar broadening, which facilitates studies of proteins that cannot be deuterated, especially in cases where production requires eukaryotic expression systems. The option of recording (15)N TROSY of proteins expressed in H2O media also alleviates the problem of incomplete amide proton back exchange, which often hampers the detection of amide groups in the core of large molecular weight proteins that are expressed in D2O culture media and cannot be refolded for amide back exchange. These results illustrate the potential of (15)NH-detected TROSY experiments as a means to exploit the high resolution offered by high field magnets near and above 1 GHz.

Indexed as

beta-CyclodextrinsDeuteriumMaltose-Binding ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein BindingSensitivity and Specificitybeta-CyclodextrinsDeuteriumMaltose-Binding ProteinsNitrogen IsotopesAmide back exchangeDeuterationHigh field magnetNitrogen detectionProtein NMRTROSY

Identifiers

PMID26497830
PMCPMC4749451
OpenAlexW1885839493

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.