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Open AccessArticle

Dynamic Nuclear Polarization of Biomembrane Assemblies

1
Department of Chemistry, University of Florida, Gainesville, FL 32611, USA
2
National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310, USA
3
Department of Biochemistry & Molecular Biology and McKnight Brain Institute, University of Florida, Gainesville, FL 32610, USA
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(9), 1246; https://doi.org/10.3390/biom10091246
Received: 14 July 2020 / Revised: 10 August 2020 / Accepted: 11 August 2020 / Published: 27 August 2020
(This article belongs to the Special Issue Advances in Membrane Proteins)
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. View Full-Text
Keywords: Dynamic Nuclear Polarization (DNP); Nuclear Magnetic Resonance (NMR); solid-state nuclear magnetic resonance (ssNMR); membrane proteins; membrane active peptides Dynamic Nuclear Polarization (DNP); Nuclear Magnetic Resonance (NMR); solid-state nuclear magnetic resonance (ssNMR); membrane proteins; membrane active peptides
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MDPI and ACS Style

Tran, N.T.; Mentink-Vigier, F.; Long, J.R. Dynamic Nuclear Polarization of Biomembrane Assemblies. Biomolecules 2020, 10, 1246. https://doi.org/10.3390/biom10091246

AMA Style

Tran NT, Mentink-Vigier F, Long JR. Dynamic Nuclear Polarization of Biomembrane Assemblies. Biomolecules. 2020; 10(9):1246. https://doi.org/10.3390/biom10091246

Chicago/Turabian Style

Tran, Nhi T.; Mentink-Vigier, Frédéric; Long, Joanna R. 2020. "Dynamic Nuclear Polarization of Biomembrane Assemblies" Biomolecules 10, no. 9: 1246. https://doi.org/10.3390/biom10091246

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