Laboratoire des BioMolécules
-------
UMR CNRS 7203 ERL INSERM U1057

 
       

Membres :
 

Daniel Abergel
Geoffrey Bodenhausen
Ludovic Carlier 
Isabelle Correia
Luminita Duma 
Fabien Ferrage
Lucie Khemtemourian 
Olivier Lequin
Emeric Miclet 
Philippe Pelupessy 
Piotr Tekely
-
Doctorants, postdoc, CDD:

Lucie Caillon
Paolo Calligari
Cyril  Charlier
Monique Chan-Huot
Anais Hoffmann
A  Mamnikam Sadasivam
Khan Shahid
Akansha Sehgal
Bruno Vitorge






 

Equipe 3:  Structure et Dynamique des Biomolécules

Res G Bodenhausen


ED:
ED 387 : iViv : Interdisciplinaire pour le vivant
ED 388 : Chimie physique et chimie analytique de Paris Centre


  > vers le site web de l'equipe

Our research group is associated with the Ecole Normale Supérieure and Pierre and Marie Curie University in Paris (France). We are attached to the Laboratory of Biomolecules - a research unit of the Centre National de la Recherche Scientifique. We stay in a close collaboration with the NMR group from Ecole Polytechnique Federale de Lausanne. Our group is specialised in liquid state (internal dynamics in biomolecules, fast proton exchange rates, cross-correlated relaxation and single scan multidimensional experiments) and solid state (for example, de- and recoupling and measurements of chemical shift anisotropies) NMR method development. We also have the experience in protein expression and purification and in magnetic resonance imaging (MRI).

Many chemists are familiar with nuclear magnetic resonance (NMR) as a simple analytical method that allows them to determine the composition, constitution and conformation of molecules. Biologists often perceive NMR as a rather laborious alternative to X-ray diffraction for the determination of protein structures. Some physicists like to think of nuclear spins as prototypical two-level quantum systems. Very few seem to be aware of the breadth and variety of applications of NMR to solids, liquids and gases. The amazing achievements of magnetic resonance imaging (MRI) are widely known, but very few understand the underlying principles. Our research group is working on various fundamental and applied aspects of NMR. Some applications are too demanding to be solved by current state-of-the-art methods, so that we may have to develop new methods before a particular problem can be tackled in a satisfactory manner. We shall give some typical examples of our work in last few years:

  • # the characterization of fast exchange of labile protons in functional groups such as amines (with rates of ca. 100 000 jumps per second),
  • # the measurement of slow rotations of aromatic rings embedded in proteins (on the order of 1 ring-flip per second),
  • # the slow rearrangements of ribonucleic acids (RNA’s) between different possible folds (a few inter-conversions per second),
  • # the determination of diffusion coefficients of macromolecules in solution (on the order of 10 -11 m2s-1, which amounts to displacements of a few micrometers per second),
  • # the study of the internal mobility of backbones and side-chains in proteins (typically from 10 2 to 10 6  events per second),
  • # the characterization of motions on a broad range of time-scales in polycrystalline samples of biomolecules (up to 10 7 jumps per second),
  • # the enhancement of weak NMR signals by dynamic nuclear polarization (DNP), both in liquids by the so-called ‘dissolution’ method and in solids by ‘in situ’ saturation of electron spin resonance,
  • # the improvement of the spectral resolution in solid-state NMR spectra of nuclei such as carbon-13 by magic angle spinning (MAS),
  • # the narrowing of carbon-13 signals through proton decoupling methods that can be combined with fast MAS,
  • # the determination of the lengths and geometry of hydrogen and halogen bonds,
  • # the indirect detection of nitrogen-14 NMR in solids in view of determining second-order quadrupolar couplings and the effects of motions on these parameters,
  • # the art of recording two-dimensional spectra in a fraction of a second, in view of monitoring exchange processes in real time.
Grants

  • Equipements d'Excellence (2011-2018): major grant (5 million Eur) for the purchase of a 800 MHz wide-bore (WB) system equipped with a gyrotron for solid-state DNP and high-field MRI (PI: G. Bodenhausen, heading a consortium with 9 partners in Paris-centre and Orléans.)
  • ERC Starting Grant 2012-2016: 2F4BIODYN, Two-field NMR spectroscopy for the exploration of biomolecular dynamics (PI: F. Ferrage)
  • ANR Jeune Chercheur 2012: COLD (PI: E. Miclet)
  • ANR Blanc 2012-2015: DYN-IDP, Proteins: the timescale of disorder (PI: F. Ferrage)
  • ANR Blanc 2011-2014: FT-ICR 2D, Two-dimensional mass spectrometry (PI: Ch. Rolando)
  • ANR Blanc 2007-2010: SAACoude, Aminoacides à conformation contrôlée: nouvelles approches stéréosélectives et application à la conception de librairies de coudes bêta (Coordinator: J. Szymoniak)
  • ANR Blanc 2009-2012: FastSpinProts, Jiggling and wigglings proteins: characterization by solid-state NMR with fast magic angle spinning (PI: G. Bodenhausen)
  • ANR Blanc 2011-2013: ParaHP, Paracrine activity and translocation of homeoproteins (Coordinator: A. Joliot, correspondant team 3 O. Lequin)
  • ANR Blanc 2011-2013: FAC, Foldzymes, foldamers targeting catalytic activity (PI: P. Karoyan team 1, correspondant team 3 O. Lequin)
  • ANR MI2 2011-2012: IMPRO-Fprau, Immuno-modulatory effects mediated by peptides derived from a specific (PI: P. Seksik team 4, correspondant team 3 O. Lequin)
  • Convergence UPMC 2011-2012: Peptides antimicrobiens et leishmaniose (Coordinator: A. Ladram)
  • Emergence UPMC 2009: RMN de protéines dans les cellules vivantes: application au facteur de transcription Engrailed (PI: O. Lequin)
  • PGG Project 2009-2011, Magnetic resonance in inhomogeneous fields: MRS and MRI from in vitro to in vivo (PI: P. Pelupessy)
  • Grant from IBISA for high-field MRI (PI: G. Bodenhausen)


Publications recentes :