ArticleChemical science2023
High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz.
Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Controlling the Guanidinium Cation Rotation by Cation-π Interactions.Angewandte Chemie (International ed. in English) · 2026Article
- Super-Resolution solid-state NMR Spectroscopy.Journal of biomolecular NMR · 2026Article
- Article
- High-qualitySolid state nuclear magnetic resonance · 2025Article
- Ultrahigh-resolution solid-state NMR for high-molecular weight proteins on GHz-class spectrometers.Science advances · 2025Article
- Proton-Detected Solid-State NMR for Deciphering Structural Polymorphism and Dynamic Heterogeneity of Cellular Carbohydrates in Pathogenic Fungi.Journal of the American Chemical Society · 2025Article
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Evaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG.Journal of biomolecular NMR · 2025Article
- Observation ofNature communications · 2024Article
- Low-power WALTZ decoupling under magic-angle spinning NMR.Magnetic resonance (Gottingen, Germany) · 2024Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NMR spectra of side-chain protons in proteins provide important information, not only about their structure and dynamics, but also about the mechanisms that regulate interactions between macromolecules. However, in the solid-state, these resonances are particularly difficult to resolve, even in relatively small proteins. We show that magic-angle-spinning (MAS) frequencies of 160 kHz, combined with a high magnetic field of 1200 MHz proton Larmor frequency, significantly improve their spectral resolution. We investigate in detail the gain for MAS frequencies between 110 and 160 kHz MAS for a model sample as well as for the hepatitis B viral capsid assembled from 120 core-protein (Cp) dimers. For both systems, we found a significantly improved spectral resolution of the side-chain region in the
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