Dynamic Nuclear Polarization of Deuterated Proteins

Author(s)
Akbey, Umit; Franks, W. Trent; Linden, Arne; Lange, Sascha; Griffin, Robert Guy; ... Show more
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Abstract
For D's a jolly good fellow: Deuteration of proteins significantly increases the signal enhancements observed in dynamic nuclear polarization (DNP) magic-angle spinning (MAS) NMR experiments. In 13C CP-MAS spectra an enhancement of 120 is observed for perdeuterated SH3 with an exchangeable proton ratio of 50 %, whereas the enhancement is only 31 for the fully protonated SH3. The direct 13C excitation of the perdeuterated sample increases the enhancement to 148.
Date issued
2010-08
URI
http://hdl.handle.net/1721.1/74582
Department
Massachusetts Institute of Technology. Department of Chemistry; Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
Journal
Angewandte Chemie International Edition
Publisher
Wiley-Blackwell Pubishers
Citation
Akbey, Ümit et al. “Dynamic Nuclear Polarization of Deuterated Proteins.” Angewandte Chemie International Edition 49.42 (2010): 7803–7806. Web.
Version: Author's final manuscript
ISSN
0570-0833
1521-3773
1433-7851
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