ArticleProceedings of the National Academy of Sciences of the United States of America2025
Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- DNP enhanced solid-state NMR of lattice-like microcrystalline protein assemblies facilitated by co-assembly with dinitroxide-tagged proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Concentration-dependent mutational scanning probes the cellular folding landscape of α-synuclein in yeast.Protein science : a publication of the Protein Society · 2026Article
- Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.The journal of physical chemistry letters · 2025Article
- Concentration-Dependent Mutational Scanning Probes the Cellular Folding Landscape of α-Synuclein in Yeast.bioRxiv : the preprint server for biology · 2025Article
- MAS Cryoprobe Enhances Solid-State NMR Signals of α-Synuclein Fibrils.bioRxiv : the preprint server for biology · 2025Article
- Paramagnetic Agents for SE DNP: Synthesis and ESR Characterization of New Lipophilic Derivatives of Finland Trityl.Molecules (Basel, Switzerland) · 2025Article
- Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- 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
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Abstract
The protein α-syn adopts a wide variety of conformations including an intrinsically disordered monomeric form and an α-helical-rich membrane-associated form that is thought to play an important role in cellular membrane processes. However, despite the high affinity of α-syn for membranes, evidence that the α-helical form is adopted inside cells has been indirect. DNP-assisted solid-state NMR on frozen cellular samples can report directly on the entire conformational ensemble. By controlling the distribution of the DNP agent throughout the cellular biomass, such experiments can provide quantitative information upon the entire structural ensemble or provide information about spatially resolved subpopulations. When the polarization agent is dispersed homogeneously throughout the cell, a minority of the α-syn inside HEK293 cells adopts a highly α-helical-rich conformation. When the polarization agent is peripherally localized, the α-helical-rich conformation predominates, indicating that it is preferentially adopted near the cellular periphery. This demonstrates how selectively altering the spatial distribution of the DNP agent can be a powerful tool to observe spatially distinct structural ensembles. This approach paves the way for more nuanced investigations into the conformations that proteins adopt in different areas of the cell.
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