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Protein NMR Spectroscopy at 150 kHz Magic‐Angle Spinning Continues To Improve Resolution and Mass Sensitivity
Author(s) -
Schledorn Maarten,
Malär Alexander A.,
Torosyan Anahit,
Penzel Susanne,
Klose Daniel,
Oss Andres,
Org MaiLiis,
Wang Shishan,
Lecoq Lauriane,
Cadalbert Riccardo,
Samoson Ago,
Böckmann Anja,
Meier Beat H.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000341
Subject(s) - laser linewidth , magic angle spinning , nuclear magnetic resonance spectroscopy , spectroscopy , resolution (logic) , spectral resolution , sensitivity (control systems) , chemistry , analytical chemistry (journal) , spectral line , magic angle , mass spectrometry , nuclear magnetic resonance , materials science , optics , physics , stereochemistry , chromatography , computer science , laser , quantum mechanics , astronomy , artificial intelligence , electronic engineering , engineering
Spectral resolution is the key to unleashing the structural and dynamic information contained in NMR spectra. Fast magic‐angle spinning (MAS) has recently revolutionized the spectroscopy of biomolecular solids. Herein, we report a further remarkable improvement in the resolution of the spectra of four fully protonated proteins and a small drug molecule by pushing the MAS rotation frequency higher (150 kHz) than the more routinely used 100 kHz. We observed a reduction in the average homogeneous linewidth by a factor of 1.5 and a decrease in the observed linewidth by a factor 1.25. We conclude that even faster MAS is highly attractive and increases mass sensitivity at a moderate price in overall sensitivity.