Presentation of the Nuclear Magnetic Resonance Lab (LRMN)

Nuclear magnetic resonance (NMR) has become an important technique for the determination of the three-dimensional structure of biological macromolecules. The ability to characterize both solution structure and dynamics, possibly in the presence of physiological partners have made NMR an essential tool for understanding biological processes. The study of molecular complexes, even in the case of weak affinity, opens up powerful opportunities for the development of pharmacologically active molecules.

Research themes

• Methodological developments
• Advanced isotopic labelling (Partnership for Structural Biology)
• Biological systems

Key words NMR (Nuclear magnetic resonance), Proteins, Biomolecules, Structure, Dynamics, Pulse Sequences, Molecular Modelling, Isotopic labelling, NMR facility

Specialised techniques NMR (Nuclear magnetic resonance), Molecular Modelling, Isotopic labelling, Molecular Biology, Protein Purification.

Specific Equipment 3 NMR spectrometers : 2x600, 1 800MHz; 2 of them equipped with cryogenically cooled probes, 1 penta-probe for 1H,13C,15N, and 31P correlation experiments.

Major publications (2007-2008)

1) Kern T, Hediger S, Muller P, Giustini C, Joris B, Bougault C, Vollmer W and Simorre JP Toward the characterization of peptidoglycan structure and protein-peptidoglycan interactions by solid-state NMR spectroscopy. Journal of the American Chemical Society (2008) 130(17): 5618-5619

2) Lescop E, Rasia R and Brutscher B Hadamard amino-acid-type edited NMR experiment for fast protein resonance assignment. Journal of the American Chemical Society (2008) 130(15): 5014-5015

3) Tarendeau F, Boudet J, Guilligay D, Mas PJ, Bougault CM, Boulo S, Baudin F, Ruigrok RW, Daigle N, Ellenberg J, Cusack S, Simorre JP and Hart DJ Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nature Structural and Molecular Biology (2007) 14(3): 229-233

4) Sounier R, Blanchard L, Wu Z and Boisbouvier J High-accuracy distance measurement between remote methyls in specifically protonated proteins. Journal of the American Chemical Society (2007) 129(3): 472-473

5) P. Schanda, V, Forge,B. Brutscher, Protein folding and unfolding studied at atomic resolution by fast 2D NMR spectroscopy, Proc. Natl. Acad. Sci. USA (2007) 104, 11257-11262.

(You can find all the publications of the laboratory here).