4.4 Article

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

Journal

CHEMBIOCHEM
Volume 21, Issue 17, Pages 2540-2548

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202000341

Keywords

fast MAS; proteins; solid-state NMR spectroscopy

Funding

  1. Estonian Science Agency [PUT 1534]
  2. French Agence Nationale de Recherche [ANR-14-CE09-0024B]
  3. LABEX ECOFECT within the Universite de Lyon program Investissements d'Avenir [ANR-11-LABX-0048, ANR-11-IDEX-0007]
  4. Swiss National Science Foundation [200020_159707]
  5. European Research Council (ERC) under the European Union [741863]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available