ArticleBiomolecules2020
Dynamic Nuclear Polarization of Biomembrane Assemblies.
Article in Biomolecules, 2020. 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.
- Effects of moisture content on the co-oxidation behavior of sturgeon myofibrillar protein and sturgeon oil.Food chemistry: X · 2026Article
- Mechanically Interlocked Double-Walled Covalent Organic Framework with Cucurbit[8]Uril-Stabilized Viologen Radical Dimers.Journal of the American Chemical Society · 2026Article
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu.Journal of biomolecular NMR · 2024Article
- Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022Review
- Stability of the nitroxide biradical AMUPol in intact and lysed mammalian cells.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Fine optimization of a dissolution dynamic nuclear polarization experimental setting forMagnetic resonance (Gottingen, Germany) · 2022Article
- In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells.Journal of the American Chemical Society · 2021Article
- Competing Transfer Pathways in Direct and Indirect Dynamic Nuclear Polarization MAS NMR Experiments on HIV-1 Capsid Assemblies: Implications for Sensitivity and Resolution.Magnetic resonance (Gottingen, Germany) · 2021Article
- Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.Frontiers in molecular biosciences · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
While atomic scale structural and dynamic information are hallmarks of nuclear magnetic resonance (NMR) methodologies, sensitivity is a fundamental limitation in NMR studies. Fully exploiting NMR capabilities to study membrane proteins is further hampered by their dilution within biological membranes. Recent developments in dynamic nuclear polarization (DNP), which can transfer the relatively high polarization of unpaired electrons to nuclear spins, show promise for overcoming the sensitivity bottleneck and enabling NMR characterization of membrane proteins under native-like conditions. Here we discuss fundamental aspects of DNP-enhanced solid-state NMR spectroscopy, experimental details relevant to the study of lipid assemblies and incorporated proteins, and sensitivity gains which can be realized in biomembrane-based samples. We also present unique insights which can be gained from DNP measurements and prospects for further development of the technique for elucidating structures and orientations of membrane proteins in native lipid environments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.