Postdoctoral positions in NMR Structural Biology - Grenoble, France

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posted: Sep 5, 2010

View of Grenoble
View of Grenoble

Two postdoctoral positions, funded by European Research Council, are available at the Structural Biology Institute in Grenoble (France) to study by real-time NMR the Folding & Mechanisms of Protein Quality Control (PQC) Machineries. Selected candidates will use latest NMR technologies developed at IBS to characterize self-assembly and functionally important structural rearrangements of large PQC machineries isolated at IBS.


About the project and the research facilities

The study of the structural and functional properties of biomolecular nanomachines remains a considerable challenge for modern structural biology. Such systems are investigated at IBS using a multifaceted approach combining X-ray crystallography and complementary low-resolution methods (e.g. SAXS, SANS or cryo-EM). These combined analyses provide valuable static pictures of the systems but rarely report the kinetic data necessary for a full, atomic resolution understanding of the mode of action. Our laboratory is using state of the art of NMR spectroscopy, isotope labeling and automated molecular biology techniques – all developed locally by the team – to characterize at atomic resolution, the off-equilibrium dynamics of such supra-molecular assemblies.

Cellular PQC mechanisms are critical for maintaining protein homeostasis and preventing the build-up of unfolded, mis-folded or unwanted proteins. The proposed approach, coupling structure and dynamics with NMR-probed real-time kinetics, will enable an holistic understanding of the activity of PQC nanomachines at the structural level. The laboratory hosts three NMR spectrometers equipped with cryogenic probes (600 MHz and 800 MHz) and with a solid state MAS equipment (600 MHz). It has access to the nearby 1 GHz NMR spectrometer of the European high field NMR centre in Lyon. Applicants will also have access to a fully-equipped wet-lab for preparation of specifically isotopically-labeled NMR samples. Grenoble is a pleasant city situated in the heart of the French alps, and has one of Europe’s most vibrant structural biology communities centered around the European Synchroton Radiation Facility (ESRF), the Laue Langevin Institute (ILL), the Structural Biology Institute (IBS) and the EMBL Grenoble Out-Station.

Candidate requirements and position benefits

We are seeking for a highly motivated candidate, with a good background and experience in biochemistry and biophysics. An ability to learn NMR techniques, high motivation, a strong publication record and fluency in English are expected. Prior experience in Biomolecular NMR will be highly appreciated but is not mandatory. Competitive salary (based on previous research experience) is offered with health insurance, retirement plan, and language training allowance.

How to apply

Interested candidates should forward a Curriculum Vitae in English, and electronic addresses of potential references via e-mail to :

Selected Publications of the team

  • Gans, Hamelin, Sounier, Ayala, Durá, Amero, Noirclerc-Savoye, Franzetti, Plevin , Boisbouvier. Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins. Angew Chem Int Ed Engl. 49:1958-62 (2010).
  • Plevin, Bryce, Boisbouvier Direct detection of CH/p interactions in proteins. Nature Chemistry. 2:466-71 (2010).
  • Amero, Schanda, Durá, Ayala, Marion, Franzetti, Brutscher, Boisbouvier. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. J Am Chem Soc.131:3448-9 (2009).
  • Ayala, Sounier, Usé, Gans, Boisbouvier. An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein. J Biomol NMR. 43:111-9 (2009).
  • Rasia, Noirclerc-Savoye, Bologna, Gallet, Plevin, Blanchard, Palatnik, Brutscher, Vernet, Boisbouvier. Parallel screening and optimization of protein constructs for structural studies. Protein Sci.18:434-9 (2009).
  • Van Melckebeke, Devany, Di Primo, Beaurain, Toulmé, Bryce, Boisbouvier. Liquid-crystal NMR structure of HIV TAR RNA bound to its SELEX RNA aptamer reveals the origins of the high stability of the complex. Proc Natl Acad Sci U S A. 105:9210-5 (2008).
  • Sounier, Blanchard, Wu, Boisbouvier High-accuracy distance measurement between remote methyls in specifically protonated proteins. J Am Chem Soc. 129:472-3. (2007).
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