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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
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
Zeitschrift
Journal of Magnetic Resonance
Quellenangaben
Band: 216,
Seiten: 1-12
Verlag
Elsevier
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)