The biomolecular NMR research group of Dr. Eric Guittet (http://www.icsn.cnrs-gif.fr/guittet
) at the Institut de Chimie des Substances Naturelles in Gif-sur-Yvette, suburb of Paris (France), is looking to recruit Master students, PhD students and postdocs from all nationalities.
Our laboratory uses modern NMR techniques to decipher the molecular mechanisms underlying biological functions for a variety of systems involving proteins such as enzymes, unfolded proteins and macromolecular complexes. We are also interested in structure-based drug design and in developing new methodology for protein NMR resonance assignment and dynamic studies of slow motions in proteins.
We are seeking candidates for the following projects:
- Investigation of the catalytic role of interdomain motion in a 60kDa enzyme. (PI Ewen Lescop)
- Analysis of the interactions of WH2/Tbeta domains with actin, investigation of their functions in the regulation of actin polymerization. (PI Carine van Heijenoort)
- Investigation of membrane proteins. (PI Eric Guittet)
- Fragment-based drug design, including methological developments. (PI Eric Guittet)
- Solid-state NMR characterization of amyloid fibrils (PI Christina Sizun)
Our laboratory offers access to several high field liquid state NMR spectrometers, including a 950 MHz, a 800MHz and two 600MHz spectrometers equipped with cryoprobes, as well as a 700MHz for dual liquid and solid-state NMR use. Our institute (ICSN) is located on the CNRS campus of Gif-sur-Yvette, a charming village with countryside flavour, 40mn away from Paris by train. The campus, which is mainly dedicated to life sciences, is part of the large scientific community located South-West of Paris, next to the Soleil synchrotron and Paris XI-Orsay University.
Highly motivated applicants with a strong background in biochemistry, biophysics and/or NMR spectroscopy are invited to apply. Please contact eric.guittet_at_icsn.cnrs-gif.fr for more information and include a CV with a summary of research interests and accomplishments.
Selected publications from the lab:
- Buosi V, Placial JP, Leroy JL, Cherfils J, Guittet E, van Heijenoort C. "Insight into the role of dynamics in the conformational switch of the small GTP-binding protein Arf1." J Biol Chem. 2010;285:37987-94
- Stratmann D, Guittet E, van Heijenoort C. Robust structure-based resonance assignment for functional protein studies by NMR. J Biomol NMR. 2010;46:157-73.
- Lescop E, Briand L, Pernollet JC, Guittet E. Structural basis of the broad specificity of a general odorant-binding protein from honeybee. Biochemistry. 2009;48:2431-41.
- Lescop E, Brutscher B. Highly automated protein backbone resonance assignment within a few hours: the "BATCH" strategy and software package. J Biomol NMR. 2009;44:43-57.
- Catoire LJ, Zoonens M, van Heijenoort C, Giusti F, Popot JL, Guittet E. Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation. J Magn Reson. 2009;197(1):91-5.
- Lescop E, Rasia R, Brutscher B. Hadamard amino-acid-type edited NMR experiment for fast protein resonance assignment.J Am Chem Soc. 2008;130:5014-5
- Carlier MF, Hertzog M, Didry D, Renault L, Cantrelle FX, van Heijenoort C, Knossow M, Guittet E. Structure, function, and evolution of the beta-thymosin/WH2 (WASP-Homology2) actin-binding module. Ann N Y Acad Sci. 2007;1112:67-75
- Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Pr
éat T, Knossow M, Guittet E, Carlier MF. The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell. 2004;117:611-23.
- Catoire LJ, Damian M, Giusti F, Martin A, van Heijenoort C, Popot JL, Guittet E, Banères JL. Structure of a GPCR ligand in its receptor-bound state: leukotriene B4 adopts a highly constrained conformation when associated to human BLT2. J Am Chem Soc. 2010;132:9049-57
- Aliprandi P, Sizun C, Perez J, Mareuil F, Caputo S, Leroy JL, Odaert B, Laalami S, Uzan M, Bontems F. S1 ribosomal protein functions in translation initiation and ribonuclease RegB activation are mediated by similar RNA-protein interactions: an NMR and SAXS analysis. J Biol Chem. 2008;283:13289-301