A Ph.D. position is available in the team of Dr. Malene R. Jensen at the Institute for Structural Biology in Grenoble, France.
The successful candidate will study the assembly of scaffolding complexes in the mitogen-activated protein kinase (MAPK) cell signalling pathways. In particular, the candidate 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 position is funded by the Bettencourt Schueller foundation through the Impulscience program.
More information can be found on the team website: www.jensen-nmr.fr
More information can be found on the team website: www.jensen-nmr.fr
Facilities
The Institute for Structural Biology 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) and the Institute Laue-Langevin (ILL). The IBS houses six high-field NMR spectrometers (3 x 600, 700, 850 and 950 MHz) and biochemistry 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 (ISBG).
Qualifications
The ideal candidate holds a degree in chemistry, biochemistry or biophysics (or related discipline) and has experience in protein expression and purification. Experience with solution NMR spectroscopy and data analysis would be a strong advantage. To apply for this position, please send your CV, a detailed motivation letter and the names of two referees on the CNRS recruitment portal. The Ph.D. thesis will start in autumn 2023.
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.
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.
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. (2020), 117, 20576-20585.
Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage
R. Schneider, M. Blackledge, M.R. Jensen. Curr. Opin. Struct. Biol. (2018) 54, 10-18.
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.
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.
Structure and dynamics of the MKK7-JNK signalling complex
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.
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.
Structure and dynamics of the MKK7-JNK signalling complex
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Dr. Malene R. Jensen | CNRS Research Director
Institut de Biologie Structurale
71, avenue des Martyrs | CS 10090 | 38044 Grenoble CEDEX 9 | Fra