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Protein NMR Spectroscopy at 150 kHz Magic-Angle Spinning Continues To Improve Resolution and Mass Sensitivity.

Maarten SchledornAlexander A MalärAnahit TorosyanSusanne PenzelDaniel KloseAndres OssMai-Liis OrgShishan WangLauriane LecoqRiccardo CadalbertAgo SamosonAnja BöckmannBeat H Meier
Published in: Chembiochem : a European journal of chemical biology (2020)
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.
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