Post doctoral position in NMR/protein dynamics Grenoble

ERC-funded postdoctoral position : Using NMR to describe the role of intrinsic disorder in viral replication assemblies

Blackledge group (Protein Dynamics and Flexibility by NMR). Institute of Structural Biology, Grenoble, France.

Project description: We are seeking a highly motivated post-doctoral researcher to exploit and/or develop NMR spectroscopic approaches to study dynamic assemblies involved in the replication of pathogenic RNA viruses, including SARS-CoV-2 and influenza.
The molecular mechanisms regulating the functional modes of intrinsically disordered proteins (IDPs) remain poorly understood. We are interested in studying the conformational dynamics of highly disordered assemblies to understand how they function. The successful candidate will investigate the role of highly dynamic proteins involved in viral replication. The project lies at the interface of biology, chemistry and physics and will exploit the exquisite sensitivity of NMR spectroscopy to investigate essential dynamic processes, in combination with fluorescence spectroscopy and imaging, X-ray crystallography, cryo-electron microscopy, small angle scattering and molecular simulation. Profile:     We are looking for candidates who are interested in using NMR to resolve fascinating biological problems. Candidates should have a PhD in chemistry, biochemistry, biophysics or a biomolecular NMR-related subject. Interested candidates should send a cv, motivation letter and the names of two referees to martin.blackledge@ibs.fr or write to martin.blackledge@ibs.fr for more details. Deadline 15th May 2022.
Grenoble: Capital of the French Alps, Grenoble is an international scientific centre with a strong international flavour. It is a pleasant city, situated at the foot of three mountain ranges offering many possibilities for cultural, outdoor and sporting activities throughout the year. Grenoble is also close to the French riviera, Italy and Switzerland and is served by international and national airports. http://www.ibs.fr/jobs/about-grenoble/
Facilities: The IBS is situated on the European Photon and Neutron (EPN) campus together with its international partners, the EMBL (European Molecular Biology Laboratory), the ESRF (European Synchrotron Radiation Facility), and the ILL (Institute Laue-Langevin). This unique site provides access to state of the art equipment to analyze biological systems at different scales of resolution.
The EPN site, and the Grenoble scientific community in general represents a true hub of integrated structural and dynamic biology.
The IBS itself provides a lively international working environment with state-of-the-art NMR facilities, including 950, 850, 700 and 3x600MHz NMR spectrometers with both liquid-state cryoprobes and state-of-the-art solid-state technology, dedicated wet-lab facilities for cloning, _expression_ and purification of proteins and state-of-the-art imaging facilities. Access to biophysical platforms is facilitated via the Integrated Structural Biology Grenoble (ISBG) platform (http://www.isbg.fr/spip.php?lang=en).   Blackledge research group:  http://www.ibs.fr/groups/protein-dynamics-and-flexibility/?lang=en
Recent publications giving examples of our recent contributions to this field
The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a. Bessa LM, Guseva S, Camacho-Zarco AR, Salvi N, Mariño Perez L, Maurin D, Botova M, Malki A, Nanao M, Jensen MR, Ruigrok R, Blackledge M*  Science Advances 8, eabm4034 (2022). Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A Camacho-Zarco AR, Kalayil S, Maurin D, Salvi N, Delaforge E, Milles S, Jensen MR, Hart DJ,  Cusack S, Blackledge M*  Nature communications 11, 1-12 (2020) Measles virus nucleo-and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. Guseva, Milles, Jensen, Salvi, Kleman, Maurin, Ruigrok, Blackledge M* Science Advances eaaz7095 (2020) A unified description of intrinsically disordered protein dynamics under physiological conditions using NMR spectroscopy. Adamski, Salvi, Magnat, Milles, Jensen, Abyzov, Moreau, Blackledge* J Am Chem Soc, 141, 17817-17829 (2019) An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function. Milles S, Jensen MR, Lazert C, Guseva S, Ivashchenko S, Communie G, Maurin D, Gerlier D, Ruigrok R,* Blackledge M* Science Advances, 4, eaat7778 (2018)       Analytical Description of NMR Relaxation Highlights Correlated Dynamics in Intrinsically Disordered Proteins. Salvi, Abyzov, Blackledge. Angew Chem Int Ed Engl. 5614020-14024 (2017) Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature Dependent NMR Relaxation. Abyzov, A., Salvi, N., Schneider, R., Maurin, D., Ruigrok R, Jensen MR, Blackledge M* J Am Chem Soc, 138, 6240–6251 (2016)    Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. Schneider R, Maurin D, Communie G, Kragelj J, Hansen F, Ruigrok R, Jensen M, Blackledge M* J Am Chem Soc 137, 1220 (2015) Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors. Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M*, Gräter F*, Lemke EA* Cell. 163, 734 (2015) Direct observation of hierarchical protein dynamics. Lewandowski J, Halse M, Blackledge M*, Emsley L* Science 348, 578 (2015) Large Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin α. Delaforge, Milles, Bouvignies, Bouvier, Boivin, Salvi, Maurin, Martel, Round, Lemke, Jensen, Hart, Blackledge* J Am Chem Soc 137,15122 (2015)
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Group Leader
Research Director CEA
Protein Dynamics and Flexibility by NMR
Director Adjoint/Deputy Director
Institut de Biologie Structurale
CAMPUS EPN
71 avenue des Martyrs
CS10090
38044 Grenoble Cedex 9;
France

martin.blackledge@ibs.fr

 

http://www.ibs.fr/groups/protein-dynamics-and-flexibility/?lang=en

Telephone: +33 457 428 554