ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.
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118 citing papers in PubMed.
- Mapping mRNA Localization and Internal Structure in Lipid Nanoparticles through Solid-State Dynamic Nuclear Polarization NMR and Proton Spin-Diffusion Modeling.Small methods · 2026Article
- Super-Resolution solid-state NMR Spectroscopy.Journal of biomolecular NMR · 2026Article
- Collecting Large Datasets of Unambiguous Structural Restraints for Protein Structure Determination by 4D Proton-Detected Solid-State NMR.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Rapid Assignment of Chemical Shifts From Crystal Structures in Solid-State NMR.Angewandte Chemie (International ed. in English) · 2026Article
- Conformation-selective detection of residues in solid proteins under magic-angle-spinning.Journal of biomolecular NMR · 2026Article
- Side-chain-selective deuterium labeling by a simple bio-expression method enhances resolution and simplifies spectra inJournal of biomolecular NMR · 2025Article
- Measuring long-range contacts in a fully protonated protein at 105 kHz magic angle spinning.Journal of biomolecular NMR · 2025Article
- Determination of key functional structures of an amorphous VHL-based SMARCA2 PROTAC.Nature communications · 2025Article
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- 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
- Half a Century of Progress: The Evolution of Wheat Germ-Based In Vitro Translation into a Versatile Protein Production Method.International journal of molecular sciences · 2025Review
- Lipidic folding pathway of α-Synuclein via a toxic oligomer.Nature communications · 2025Article
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- Resolving Structures of Paramagnetic Systems in Chemistry and Materials Science by Solid-State NMR: The Revolving Power of Ultra-Fast MAS.Angewandte Chemie (International ed. in English) · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Homonuclear J-couplings and heteronuclear structural constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024Article
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58 more citing papers are in PubMed but not listed here.
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Authors and funding
17 authors.
Funding
Abstract
Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we show in two fully protonated proteins that, at 100-kHz MAS and above, spectral resolution is high enough to detect resolved correlations from amide and side-chain protons of all residue types, and to reliably measure a dense network of (1)H-(1)H proximities that define a protein structure. The high data quality allowed the correct identification of internuclear distance restraints encoded in 3D spectra with automated data analysis, resulting in accurate, unbiased, and fast structure determination. Additionally, we find that narrower proton resonance lines, longer coherence lifetimes, and improved magnetization transfer offset the reduced sample size at 100-kHz spinning and above. Less than 2 weeks of experiment time and a single 0.5-mg sample was sufficient for the acquisition of all data necessary for backbone and side-chain resonance assignment and unsupervised structure determination. We expect the technique to pave the way for atomic-resolution structure analysis applicable to a wide range of proteins.
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