Our research group is working on various fundamental and applied aspects of NMR, focusing on developments of new methods for nuclear magnetic resonance (NMR) in solution, solids and gases, and for magnetic resonance imaging (MRI) using state-of-the-art equipment.
In solution, we study internal dynamics, structure and interactions of biomolecules such as proteins and nucleic acids, based on extensive know-how in protein expression and purification. We determine fast proton exchange rates, study cross-correlated relaxation effects, develop single-scan multidimensional methods, field-dependent relaxation (“relaxometry”) using fast shuttling of samples, drug screening, and dynamic nuclear polarisation (DNP) using rapid heating of samples polarized at 1.2 K, dissolution and transfer to liquid-state spectrometers .
In solids, we investigate proteins and their complexes and porous materials that are relevant for heterogenous catalysis. We develop efficient solid-state NMR methods for measurements of chemical shift anisotropies (CSA), decoupling in samples spinning at the magic angle (MAS), for recoupling of interactions such as dipole-dipole couplings that can be retrieved despite MAS, and signal enhancement by dynamic nuclear polarisation (DNP) using microwaves generated by gyrotrons.
In gas phase we have investigated absorption and deposition of xenon and relaxation of protons in water vapour.
Our research group is associated with the Ecole Normale Supérieure and the Université Pierre and Marie Curie in Paris (France). We are part of the Laboratory of Biomolecules – a research unit (UMR 7203) of the Centre National de la Recherche Scientifique. Part of our equipment is supported by a national network Infrastructures de recherche de RMN à très habits champs (IR-RMN-THE) of the CNRS. We maintain a close collaboration with the NMR group (LRMB) at Ecole Polytechnique Fédérale de Lausanne.
For more information about us visit Paris en Resonance web site.