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Dynamic Nuclear Polarization of Deuterated Proteins

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Akbey Oschkinat Manuscript English.pdf

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Author(s)
Akbey, Umit
•
Franks, W. Trent
•
Linden, Arne
•
Lange, Sascha
•
Griffin, Robert Guy
•
van Rossum, Barth-Jan
•
Oschkinat, Harmut
Date Issued
August 2010
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
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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike 3.0
http://creativecommons.org/licenses/by-nc-sa/3.0/
Persistent DSpace Link
http://hdl.handle.net/1721.1/74582
DOI of Published Version
https://doi.org/10.1002/anie.201002044
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