Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy
RIS ID
69527
Abstract
In the past decade solid-state magic-angle-spinning (MAS) NMR spectroscopy has emerged as a unique technique for obtaining information on the atomic-level structure and dynamics of complex biological macromolecules, which owing to their properties or size are accessible neither to X-ray crystallography nor to solution NMR spectroscopy. A small number of structures has been determined by solid-state NMR spectroscopy to date, ranging from microcrystalline samples to fibrils and membrane-associated systems. Despite rapid acceptance in the biomolecular field, however, these determinations are far from being routine.
Publication Details
Marchetti, A., Jehle, S., Felletti, M., Knight, M. J., Wang, Y., Xu, Z., Park, A., Otting, G., Lesage, A., Emsley, L., Dixon, N. E. & Pintacuda, G. (2012). Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy. Angewandte Chemie - International Edition, 51 (43), 10756-10759.