Dynamic Nuclear Polarization of Deuterated Proteins

被引：137

作者：

Akbey, Uemit ^{[1
]}

Franks, W. Trent ^{[1
]}

Linden, Arne ^{[1
]}

Lange, Sascha ^{[1
]}

Griffin, Robert G. ^{[2
,3
]}

van Rossum, Barth-Jan ^{[1
]}

Oschkinat, Hartmut ^{[1
]}

机构：

[1] Leibniz Inst Mol Pharmacol FMP, NMR Supported Struct Biol, D-13125 Berlin, Germany

[2] MIT, Francis Bitter Magnet Lab, Cambridge, MA 02139 USA

[3] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 42期

关键词：

analytical methods; dynamic nuclear polarization; high-temperature DNP; perdeuterated compounds; solid-state NMR spectroscopy; NMR-SPECTROSCOPY; MOLECULAR-STRUCTURE; AMYLOID FIBRILS; MAS SPECTRA; C-13; NMR; MEMBRANE; PEPTIDE;

D O I：

10.1002/anie.201002044

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：7803 / 7806

页数：4

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