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Dr. Guido Pintacuda - Fast magic-angle spinning NMR of membrane proteins

Dr. Guido Pintacuda

Centre de RMN à Très Hauts Champs, CNRS/Université Claude Bernard Lyon 1/Ecole Normale Supérieure de Lyon, Villeurbanne, France

Fast magic-angle spinning NMR of membrane proteins

Building on a decade of continuous advances of the community, the recent development of very fast (60 kHz and above) magic-angle spinning (MAS) probes has revolutionised the field of solid-state NMR. Today, rapid “fingerprinting” of proteins by 1H detection is possible with a ten-fold reduction of the required sample amounts with respect to conventional approaches, not only in deuterated molecules but also in fully-protonated substrates. Extensive and robust resonance assignments can be derived rapidly for small-to-medium sized proteins (up to ca. 300 residues), opening the way to the determination of inter-nuclear proximities, relative orientations of secondary structural elements, protein-cofactor interactions, local and global dynamics.

Fast MAS and 1H detection techniques have nowadays been shown to be applicable to membrane-bound systems. This talk reviews the strategies underlying this recent leap forward in sensitivity and resolution, describing its potential for the detailed characterization of membrane proteins in lipid bilayers.

Sélections de publications

  • T. Schubeis, T. Le Marchand, C. Daday, W. Kopec, K.T. Movellan, J. Stanek, T.S. Schwarzer, K Castiglione, B.L. de Groot, G. Pintacuda, and L. B. Andreas (2020) A β-Barrel for Oil Transport through Lipid Membranes: Dynamic NMR Structures of AlkL Proc Natl Acad Sci USA 117, 21014–21
  • J. Stanek, T. Schubeis, P. Paluch., P. Güntert, L. Andreas, and G. Pintacuda (2020) Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition J Am Chem Soc 142, 5793-5799
  • T. Schubeis, T. Le Marchand, L. B. Andreas, G. Pintacuda (2018) 1H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins J Magn Reson 287, 140-152
  • J. S. Retel, A. J. Nieuwkoop, M. Hiller, V. A. Higman, E. Barbet-Massin, J. Stanek, L. B. Andreas, W. T. Franks, B. J. van Rossum, K. R. Vinothkumar, L. Handel, G. G. de Palma, B. Bardiaux, G. Pintacuda, L. Emsley, W. Kuhlbrandt, & H. Oschkinat (2017) Structure of outer membrane protein G in lipid bilayers Nat Commun 8, 2073
  • D. Lalli, M. Idso, L. B. Andreas, S. Hussain, N. Baxter, S. Han, B. F. Chmelkaand G. Pintacuda (2017) Proton-based structural analysis of a heptahelical transmembrane protein in lipid bilayers J Am Chem Soc 139, 13006-13012
  • O. Saurel, I. Iordanov, G. Nars, P. Demange, T. Le Marchand, L. B. Andreas, G. Pintacuda, A. Milon (2017) Local and global dynamics in Klebsiella pneumoniae outer membrane protein A in lipid bilayers probed at atomic resolution J Am Chem Soc 139, 1590-1597
  • J. Stanek, L. B. Andreas, K. Jaudzems, D. Cala, D. Lalli, A. Bertarello, T. Schubeis, I. Akopjana, S. Kotelovica, K. Tars, A. Pica, S. Leone, D. Picone, Z.-Q. Xu, N. E. Dixon, D. Martinez, M. Berbon, N. El Mammeri, A. Noubhani, S. Saupe, B. Habenstein, A. Loquet, G. Pintacuda (2016) Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils Angew Chem Int Ed Engl 55, 15504-15509; Angew Chem 128, 15730-15735 (frontispice article)
  • L. B. Andreas, K. Jaudzems, J. Stanek, D. Lalli, A. Bertarello, T. Le Marchand, D. Cala-De Paepe, S. Kotelovica, I. Akopjana, B. Knott, S. Wegner, F. Engelke, A. Lesage, L. Emsley, K. Tars, T. Herrmann, and G. Pintacuda (2016) Structure of fully protonated proteins by proton-detected magic-angle spinning NMR Proc Natl Acad Sci USA 113, 9187-9192


Contact: Olivier Saurel (

Lien pour suivre le séminaire:

2 Mar

11:00 - 12:00

Online seminar