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NMR spectroscopy provides invaluable insights into the structural and dynamical features of biomolecular systems. It is particularly well suited to analyze multiple functional states, internal flexibility and interaction processes involving proteins at an atomic scale.

 Main application field: Structure, dynamics and interactions of biomolecular systems; Analysis of small amount of small molecules (especially natural products)


 ICSN: Five spectrometers (2*600MHz, 700MHz, 800MHz and 950MHz). For more details on these spectrometers, go to:

 CEA iBiTeC-S/I2BC: Two spectrometers (600MHz and 700MHz Bruker Avance III spectrometers, equipped with TCI(1H,13C, 15N,2H) 5mm, z-gradients cryoprobes), go to:


Barrault MB, Richet N, Godard C, Murciano B, Le Tallec B, Rousseau E, Legrand P, Charbonnier JB, Le Du MH, Guérois R, Ochsenbein F, Peyroche A. Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunitsduring the proteasome assembly. Proc Natl Acad Sci U S A. 2012 Apr 24;109(17):E1001-10. 

Jiao Y, Seeger K, Lautrette A, Gaubert A, Mousson F, Guerois R, Mann C,Ochsenbein F. Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction. Proc Natl Acad Sci U S A. 2012 Feb 21;109(8):2866-71.

Other NMR laboratories with expertise in NMR in South Paris

FRISBI South Paris node has partnerships with the NMR Platform of the Genopole

 (see their web site