
Open access
Date
2019-07-24Type
- Journal Article
Citations
Cited 18 times in
Web of Science
Cited 20 times in
Scopus
ETH Bibliography
yes
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Abstract
We sequentially assigned the fully-protonated capsids made from core proteins of the Hepatitis B virus using proton detection at 100 kHz magic-angle spinning (MAS) in 0.7 mm rotors and compare sensitivity and assignment completeness to previously obtained assignments using carbon-detection techniques in 3.2 mm rotors and 17.5 kHz MAS. We show that proton detection shows a global gain of a factor ~50 in mass sensitivity, but that signal-to-noise ratios and completeness of the assignment was somewhat higher for carbon-detected experiments for comparable experimental times. We also show that deuteration and HN back protonation improves the proton linewidth at 100 kHz MAS by a factor of 1.5, from an average of 170–110 Hz, and by a factor of 1.3 compared to deuterated capsids at 60 kHz MAS in a 1.3 mm rotor. Yet, several HN protons cannot be back-exchanged due to solvent inaccessibility, which results in a total of 15% of the amides missing in the spectra. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000355162Publication status
publishedExternal links
Journal / series
Frontiers in Molecular BiosciencesVolume
Pages / Article No.
Publisher
Frontiers MediaSubject
Solid-state NMR; Fast MAS; Proton detection; Carbon detection; Deuteration; Hepatitis B virus; Capsid; Core proteinOrganisational unit
02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.03496 - Meier, Beat H. / Meier, Beat H.
Funding
159707 - NMR studies in the Solid State (SNF)
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Show all metadata
Citations
Cited 18 times in
Web of Science
Cited 20 times in
Scopus
ETH Bibliography
yes
Altmetrics