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Open Access Green as soon as Postprint is submitted to ZB.
Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for structure and dynamics.
J. Magn. Reson. 216, 1-12 (2012)
High resolution proton spectra are obtained in MAS solid-state NMR in case samples are prepared using perdeuterated protein and D(2)O in the recrystallization buffer. Deuteration reduces drastically (1)H, (1)H dipolar interactions and allows to obtain amide proton line widths on the order of 20 Hz. Similarly, high-resolution proton spectra of aliphatic groups can be obtained if specifically labeled precursors for biosynthesis of methyl containing side chains are used, or if limited amounts of H(2)O in the bacterial growth medium is employed. This review summarizes recent spectroscopic developments to access structure and dynamics of biomacromolecules in the solid-state, and shows a number of applications to amyloid fibrils and membrane proteins.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Magic Angle Spinning (MAS) solid-state NMR; Perdeuteration; 2H labeling; Microcrystalline proteins; 15N relaxation; Order parameters; Protein dynamics; ANGLE-SPINNING NMR; NUCLEAR-MAGNETIC-RESONANCE; CHEMICAL-SHIFT ANISOTROPY; ESCHERICHIA-COLI THIOREDOXIN; BETA-AMYLOID FIBRILS; SIDE-CHAIN DYNAMICS; MODEL-FREE APPROACH; BACKBONE DYNAMICS; CORRELATION SPECTROSCOPY; ORDER PARAMETERS
ISSN (print) / ISBN
1090-7807
e-ISSN
1096-0856
Journal
Journal of Magnetic Resonance
Quellenangaben
Volume: 216,
Pages: 1-12
Publisher
Elsevier
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)