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Proton-detection in biological MAS solid-state NMR spectroscopy.

In: Modern Magnetic Resonance. 2018. 879-910
DOI Verlagsversion bestellen
In the last years, proton-detected experiments became more and more routine in MAS solid-state NMR. High-resolution proton spectra are obtained in MAS solid-state NMR in case samples are prepared using perdeuterated protein and D2O in the recrystallization buffer. Deuteration reduces drastically1H,1H 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 H2O 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, membrane proteins, and soluble protein complexes.
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Publikationstyp Artikel: Sammelbandbeitrag/Buchkapitel
Schlagwörter 15 N Relaxation ; 2 H Labeling ; Magic Angle Spinning (mas) Solid-state Nmr ; Microcrystalline Proteins ; Order Parameters ; Perdeuteration ; Protein Dynamics
ISSN (print) / ISBN 9783319283883
Bandtitel Modern Magnetic Resonance
Quellenangaben Band: , Heft: , Seiten: 879-910 Artikelnummer: , Supplement: ,