ArticleProceedings of the National Academy of Sciences of the United States of America2022
Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Solution-state nuclear magnetic resonance studies of theBiochemistry and biophysics reports · 2026Article
- Top-Down Scoring of Spectral Fitness by Image Analysis for Protein Structure Validation.Journal of chemical information and modeling · 2026Article
- Backbone assignment of a 28.5 kDa class A extended spectrum β-lactamase by high-field, carbon-detected solid-state NMR.Biomolecular NMR assignments · 2025Article
- High-dimensional solid-state NMR facilitated by transverse-mixing optimal control.Research square · 2025Article
- Ultrahigh-resolution solid-state NMR for high-molecular weight proteins on GHz-class spectrometers.Science advances · 2025Article
- OPTO: Automated Optimization for Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Spiers Memorial Lecture: NMR crystallography.Faraday discussions · 2025Article
- The interplay of density functional selection and crystal structure for accurate NMR chemical shift predictions.Faraday discussions · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Sedimentation of large, soluble proteins up to 140 kDa forJournal of biomolecular NMR · 2024Article
- Integrating molecular dynamics simulation with small- and wide-angle X-ray scattering to unravel the flexibility, antigen-blocking, and protease-restoring functions in a hindrance-based pro-antibody.Protein science : a publication of the Protein Society · 2024Article
- Studying large biomolecules as sedimented solutes with solid-state NMR.Biophysics reports · 2024Article
- Solid-State NMRJournal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Protein deuterationChemical communications (Cambridge, England) · 2024Article
- Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase.Cell reports. Physical science · 2024Article
- Molecular mechanisms and evolutionary robustness of a color switch in proteorhodopsins.Science advances · 2024Article
- Deuteration of proteins boosted by cell lysates: high-resolution amide and HMagnetic resonance (Gottingen, Germany) · 2024Article
- 5D solid-state NMR spectroscopy for facilitated resonance assignment.Journal of biomolecular NMR · 2023Article
- High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz.Chemical science · 2023Article
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12 authors.
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Abstract
NMR chemical shifts provide detailed information on the chemical properties of molecules, thereby complementing structural data from techniques like X-ray crystallography and electron microscopy. Detailed analysis of protein NMR data, however, often hinges on comprehensive, site-specific assignment of backbone resonances, which becomes a bottleneck for molecular weights beyond 40 to 45 kDa. Here, we show that assignments for the (2x)72-kDa protein tryptophan synthase (665 amino acids per asymmetric unit) can be achieved via higher-dimensional, proton-detected, solid-state NMR using a single, 1-mg, uniformly labeled, microcrystalline sample. This framework grants access to atom-specific characterization of chemical properties and relaxation for the backbone and side chains, including those residues important for the catalytic turnover. Combined with first-principles calculations, the chemical shifts in the β-subunit active site suggest a connection between active-site chemistry, the electrostatic environment, and catalytically important dynamics of the portal to the β-subunit from solution.
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