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Updated: Feb 27, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
Published on: November 2, 2018
Compensating the asymmetric probe response in broad MAS NMR spectra of quadrupolar nuclei
Pedro B Groszewicz1, Hergen Breitzke1, Gerd Buntkowsky1
1Institute of Physical Chemistry, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Abstract:
The spinning sidebands envelope of satellite transitions often display an asymmetric shape, which is caused by an asymmetric response of the NMR probe circuit. In this work, we revisit the basic concepts of the RLC circuit at the heart of every NMR probe and present two approaches capable of minimizing this artifact. While the first one consists of deliberately mistuning the probe, the second one relies on measuring the probe's response function and deconvoluting its contribution from the spectra. Both approaches are validated with 23Na NMR spectra of a lead-free relaxor ferroelectric (BNT-1BT). This material is particularly suitable as an example of the applicability of both strategies for samples with a disordered local structure.
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