Two postdoctoral positions are available in the team of Dr. Malene R. Jensen at the Institute for Structural Biology in Grenoble, France.
The successful candidates will study the assembly of scaffolding complexes in the mitogen-activated protein kinase (MAPK) cell signalling pathways. In particular, the candidates will characterise the structure, dynamics and interactions of intrinsically disordered scaffold proteins and elucidate how liquid-liquid phase separation contributes to MAPK enzymatic activity. The group uses NMR spectroscopy and X-ray crystallography in combination with biophysical techniques. The positions are available from the 1st of January 2023, initially for 2 years with a possible extension of up to 4 years. More information can be found on the team website: www.jensen-nmr.fr <http://www.jensen-nmr.fr/> Facilities The Institute for Structural Biology <http://www.ibs.fr/spip.php?lang=en> is located on the EPN science campus in Grenoble in close proximity to the European Synchrotron Radiation Facility (ESRF), the European Molecular Biology Laboratory (EMBL) Grenoble Outstation and the Institute Laue-Langevin (ILL). The IBS houses six high-field NMR spectrometers (3 x 600, 700, 850 and 950 MHz) and wetlab facilities for cloning, expression and purification of proteins. Access is facilitated to a number of state-of-the-art research platforms through Integrated Structural Biology Grenoble <https://www.isbg.fr/?lang=en>. Qualifications The ideal candidate holds a PhD in chemistry, biochemistry or biophysics (or related discipline) and has experience in protein expression and purification and a proven track-record in solution NMR spectroscopy and/or X-ray crystallography. To apply for this position, please send your CV, a motivation letter and the names of two references to malene.ringkjobing-jen...@ibs.fr <mailto:malene.ringkjobing-jen...@ibs.fr> Recent relevant publications L. Mariño Pérez, F.S. Ielasi, L.M. Bessa, D. Maurin, J. Kragelj, M. Blackledge, N. Salvi, G. Bouvignies, A. Palencia, M.R. Jensen Nature (2022), 602, 695-700. <https://www.nature.com/articles/s41586-022-04417-6> Visualizing protein breathing motions associated with aromatic ring flipping J. Kragelj, T. Orand, E. Delaforge, L. Tengo, M. Blackledge, A. Palencia, M.R. Jensen Biomolecules (2021),11,1204. <https://www.mdpi.com/2218-273X/11/8/1204> Enthalpy-entropy compensation in the promiscuous interaction of an intrinsically disordered protein with homologous protein partners K.K. Rasmussen, A. Palencia, A.K. Varming, H. El-Wali, E. Boeri Erba, M. Blackledge, K. Hammer, T. Herrmann, M. Kilstrup, L. Lo Leggio, M.R. Jensen Proc. Natl. Acad. Sci. U.S.A. (2020) 117, 20576-20585. <https://www.pnas.org/doi/10.1073/pnas.2005218117> Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage R. Schneider, M. Blackledge, M.R. Jensen Curr. Opin. Struct. Biol. (2019) 54, 10-18. <https://www.sciencedirect.com/science/article/pii/S0959440X1830054X?via=ihub> Elucidating binding mechanisms and dynamics of intrinsically disordered protein complexes using NMR spectroscopy E. Delaforge, J. Kragelj, L. Tengo, A. Palencia, S. Milles, G. Bouvignies, N. Salvi, M. Blackledge, M.R. Jensen J. Am. Chem. Soc. (2018) 140, 1148-1158. <https://pubs.acs.org/doi/abs/10.1021/jacs.7b12407> Deciphering the dynamic interaction profile of an intrinsically disordered protein by NMR exchange spectroscopy J. Kragelj, A. Palencia, M. Nanao, D. Maurin, G. Bouvignies, M. Blackledge, M.R. Jensen Proc. Natl. Acad. Sci. (2015) 112, 3409-3414. <https://www.pnas.org/doi/10.1073/pnas.1419528112> Structure and dynamics of the MKK7-JNK signalling complex -- Dr. Malene Ringkjøbing Jensen Research Director CNRS Institut de Biologie Structurale 71, avenue des Martyrs CS 10090 38044 Grenoble CEDEX 9 France ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
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