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Backbone assignment of fully protonated solid proteins by 1H detection and ultrafast magic-angle-spinning NMR spectroscopy
Faculty of Science - Papers (Archive)
  • 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 Wollongong
  • Zhi-Qiang Xu, University of Wollongong
  • 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 Wollongong
  • Guido Pintacuda, University of Lyon
RIS ID
69527
Publication Date
1-1-2012
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.

Citation Information
Alessandro 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/