ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2017
Optimized fast mixing device for real-time NMR applications.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed.
- Quantifying outer membrane permeability to β-lactam antibiotics using outer membrane vesicles that protect antibiotic-susceptible bacteria.Nature communications · 2026Article
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Analysis of conformational exchange processes using methyl-TROSY-based Hahn echo measurements of quadruple-quantum relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
- RNA Dynamics by NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2019Review
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Authors and funding
4 authors.
Funding
Abstract
We present an improved fast mixing device based on the rapid mixing of two solutions inside the NMR probe, as originally proposed by Hore and coworkers (J. Am. Chem. Soc. 125 (2003) 12484-12492). Such a device is important for off-equilibrium studies of molecular kinetics by multidimensional real-time NMR spectrsocopy. The novelty of this device is that it allows removing the injector from the NMR detection volume after mixing, and thus provides good magnetic field homogeneity independently of the initial sample volume placed in the NMR probe. The apparatus is simple to build, inexpensive, and can be used without any hardware modification on any type of liquid-state NMR spectrometer. We demonstrate the performance of our fast mixing device in terms of improved magnetic field homogeneity, and show an application to the study of protein folding and the structural characterization of transiently populated folding intermediates.
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Registered trials
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