Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy

Authors

Alessandro Marchetti, University Of Lyon
Stefan Jehle, University of Lyon
Michele Felletti, University of Lyon
Michael J. Knight, University Of Lyon
Yao Wang, University of WollongongFollow
Zhi-Qiang Xu, University of WollongongFollow
Ah-Young Park, Australian National University
Gottfried Otting, Australian National University
Anne Lesage, University of Lyon
Lyndon Emsley, University of Lyon
Nicholas E. Dixon, University of WollongongFollow
Guido Pintacuda, University of Lyon

RIS ID

69527

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.

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.