Dynamic Nuclear Polarization of Deuterated Proteins

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 prot...

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Published inAngewandte Chemie (International ed.) Vol. 49; no. 42; pp. 7803 - 7806
Main Authors Akbey, Ümit, Franks, W. Trent, Linden, Arne, Lange, Sascha, Griffin, Robert G, van Rossum, Barth-Jan, Oschkinat, Hartmut
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 11.10.2010
WILEY-VCH Verlag
WILEY‐VCH Verlag
Subjects
analytical methods
Deuterium - chemistry
dynamic nuclear polarization
high-temperature DNP
Microwaves
Nuclear Magnetic Resonance, Biomolecular - methods
perdeuterated compounds
Protein Conformation
Proteins - chemistry
solid-state NMR spectroscopy
Spectrin - chemistry
Temperature
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Summary: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.
Bibliography:http://dx.doi.org/10.1002/anie.201002044
ark:/67375/WNG-KLB6GLHM-S
ArticleID:ANIE201002044
Anne Diehl and Kristina Rehbein are gratefully acknowledged for the preparation of perdeuterated SH3 samples at different protonation levels.
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ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201002044