ArticleJournal of biomolecular NMR2024
DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu.
Article in Journal of biomolecular NMR, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Bimodal Cholesterol for Correlative In-Cell DNP Solid-State NMR and Confocal Microscopy of the Plasma Membrane.Journal of the American Chemical Society · 2026Article
- Targeted NMR signal enhancement of RNA by site-directed bis-nitroxide labeling.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Targeting Cellular Lipid Rafts for Dynamic Nuclear Polarization Nuclear Magnetic Resonance.Chembiochem : a European journal of chemical biology · 2026Article
- Pushing Sensitivity and Specificity Limits in Native Structural Biology:Journal of the American Chemical Society · 2025Article
- Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.bioRxiv : the preprint server for biology · 2024Article
- In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils.bioRxiv : the preprint server for biology · 2024Article
- Sorbitol-Based Glass Matrices Enable Dynamic Nuclear Polarization beyond 200 K.The journal of physical chemistry letters · 2024Article
- Additive fabrication for NMR probe builders.Progress in nuclear magnetic resonance spectroscopyReview
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5 authors.
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Abstract
With the sensitivity enhancements conferred by dynamic nuclear polarization (DNP), magic angle spinning (MAS) solid state NMR spectroscopy experiments can attain the necessary sensitivity to detect very low concentrations of proteins. This potentially enables structural investigations of proteins at their endogenous levels in their biological contexts where their native stoichiometries with potential interactors is maintained. Yet, even with DNP, experiments are still sensitivity limited. Moreover, when an isotopically-enriched target protein is present at physiological levels, which typically range from low micromolar to nanomolar concentrations, the isotope content from the natural abundance isotopes in the cellular milieu can outnumber the isotope content of the target protein. Using isotopically enriched yeast prion protein, Sup35NM, diluted into natural abundance yeast lysates, we optimized sample composition. We found that modest cryoprotectant concentrations and fully protonated environments support efficient DNP. We experimentally validated theoretical calculations of the limit of specificity for an isotopically enriched protein in natural abundance cellular milieu. We establish that, using pulse sequences that are selective for adjacent NMR-active nuclei, proteins can be specifically detected in cellular milieu at concentrations in the hundreds of nanomolar. Finally, we find that maintaining native stoichiometries of the protein of interest to the components of the cellular environment may be important for proteins that make specific interactions with cellular constituents.
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