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Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for structure and dynamics.

J. Magn. Reson. 216, 1-12 (2012)
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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
Quellenangaben Band: 216, Heft: , Seiten: 1-12 Artikelnummer: , Supplement: ,
Verlag Elsevier
Begutachtungsstatus Peer reviewed