Slow Molecular Motions in Ionic Liquids Probed by Cross-Relaxation of Nuclear Spins During Overhauser Dynamic Nuclear Polarization

2016 ◽  
Vol 128 (47) ◽  
pp. 14976-14981 ◽  
Author(s):  
Abhishek Banerjee ◽  
Arnab Dey ◽  
Narayanan Chandrakumar
Keyword(s):  
Ionic Liquids ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Cross Relaxation ◽  
Molecular Motions ◽  
Nuclear Spins

Heteronuclear Cross-Relaxation under Solid-State Dynamic Nuclear Polarization

2016 ◽  
Vol 138 (51) ◽  
pp. 16572-16575 ◽  
Author(s):  
Diane Daube ◽  
Victoria Aladin ◽  
Jörg Heiliger ◽  
Johannes J. Wittmann ◽  
Dominic Barthelmes ◽  
...  
Keyword(s):  
Solid State ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Cross Relaxation ◽  
State Dynamic

scholarly journals Dynamic Nuclear Polarization of Biomembrane Assemblies

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1246
Author(s):  
Nhi T. Tran ◽  
Frédéric Mentink-Vigier ◽  
Joanna R. Long
Keyword(s):  
Membrane Proteins ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Atomic Scale ◽  
Nuclear Spins ◽  
Nmr Studies ◽  
Nmr Characterization ◽  
Recent Developments ◽  
Lipid Assemblies

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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