ArticleJournal of biomolecular NMR2014
A probe to monitor performance of ¹⁵N longitudinal relaxation experiments for proteins in solution.
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 3 papers.
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.
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.
Who cites it
3 citing papers in PubMed.
- Pitfalls in measurements of RJournal of biomolecular NMR · 2025Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- An optimized method for (15)N R(1) relaxation rate measurements in non-deuterated proteins.Journal of biomolecular NMR · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
The magnitude of the ¹⁵N longitudinal relaxation rate typically decreases as magnetic field strength increases in globular proteins in solution. Thus, it is important to test the performance of ¹⁵N longitudinal relaxation experiments at high field strength. Herein, a tool to investigate systematic errors in ¹⁵N longitudinal relaxation rate, R₁, is introduced. The tool, a difference in R₁ values between the two components of the ¹H-coupled ¹⁵N magnetizations, R₁(1)-R₁(2), conveniently detects inefficiencies in cancellation of cross correlation between ¹H-¹⁵N dipolar coupling and ¹⁵N chemical shift anisotropy. Experiments, in varying conditions, and simulations of a two-spin system indicate that insufficient cancellation of the cross correlation is due to (1) ¹H pulse imperfection and (2) ¹H off-resonance effect, and (3) is further amplified by residual ¹⁵N transverse magnetization that is caused by the ¹⁵N off-resonance effect. Results also show that this problem can be easily and practically remedied by discarding the initial decay points when recording ¹⁵N longitudinal relaxation in proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.