Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopyFaculty of Science - Papers (Archive)
AbstractIn 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.
Citation InformationAlessandro Marchetti, Stefan Jehle, Michele Felletti, Michael J Knight, et al.. "Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy" (2012) p. 10756 - 10759
Available at: http://works.bepress.com/nick_dixon/46/