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Open Access Green as soon as Postprint is submitted to ZB.
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins.
J. Biomol. NMR 52, 31-39 (2012)
Biological solid-state nuclear magnetic resonance spectroscopy developed rapidly in the past two decades and emerged as an important tool for structural biology. Resonance assignment is an essential prerequisite for structure determination and the characterization of motional properties of a molecule. Experiments, which rely on carbon or nitrogen detection, suffer, however, from low sensitivity. Recently, we introduced the RAP (Reduced Adjoining Protonation) labeling scheme, which allows to detect backbone and sidechain protons with high sensitivity and resolution. We present here a (1)H-detected 3D (H)CCH experiment for assignment of backbone and sidechain proton resonances. Resolution is significantly improved by employing simultaneous (13)CO and (13)Cβ J-decoupling during evolution of the (13)Cα chemical shift. In total, ~90% of the (1)Hα-(13)Cα backbone resonances of chicken α-spectrin SH3 could be assigned.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Magic angle spinning (MAS) solid-state NMR; Perdeuteration; 2H-labeling; Side chain assignment strategies
ISSN (print) / ISBN
0925-2738
e-ISSN
1573-5001
Journal
Journal of Biomolecular NMR
Quellenangaben
Volume: 52,
Issue: 1,
Pages: 31-39
Publisher
Springer
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)