*A Ph.D. position is available in the group of Dr. Malene R. Jensen at
the Institute for Structural Biology in Grenoble, France. *
The successful candidate will combine X-ray crystallography, NMR
spectroscopy and protein engineering to study how mitogen-activated
protein kinases (MAPKs) recognize intrinsically disordered substrates.
In particular, the successful candidate will obtain structural and
dynamic snapshots of substrates at the active site of MAPKs to open new
avenues for the development of substrate-competitive inhibitors. The
position is fully funded by the CEA
<https://www.theses-postdocs.cea.fr/job/job-structural-snapshots-of-a-substrate-within-the-active-site-of-a-mitogen-activated-protein-kinase_38266.aspx>.
More information can be found on the group 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, close 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 provided to a number of state-of-the-art research platforms through
Integrated Structural Biology Grenoble <https://www.isbg.fr> (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 X-ray crystallography
and/or solution NMR spectroscopy would be an advantage. To apply for
this position, please send your CV, a detailed motivation letter and the
names and contact information of two references to
[email protected]. The Ph.D. project will start in October 2026.
*Recent publications of the group:*
Kjaer et al. Nature Commun. <https://doi.org/10.1038/s41467-025-66420-5>
(2025)
Hierarchical folding-upon-binding of an intrinsically disordered protein
Orand et al. Adv. Sci. <https://doi.org/10.1002/advs.202503987> (2025)
Sequence- and docking-site-dependent contributions to multi-site
phosphorylation of an intrinsically disordered MAPK substrate
Orand et al. PNAS <https://doi.org/10.1073/pnas.2419915122> (2025)
Bipartite binding of the intrinsically disordered scaffold protein JIP1
to the kinase JNK1
Mariño Pérez et al. Nature
<https://www.nature.com/articles/s41586-022-04417-6> (2022).
Visualizing protein breathing motions associated with aromatic ring flipping
Delaforge et al. J. Am. Chem. Soc.
<https://pubs.acs.org/doi/abs/10.1021/jacs.7b12407>(2018)
Deciphering the dynamic interaction profile of an
intrinsically disordered protein by NMR exchange spectroscopy
--
Malene R. Jensen, Ph.D.
Group leader, CNRS Research Director
Institut de Biologie Structurale
71, avenue des Martyrs | CS 10090 | 38044 Grenoble CEDEX 9 | France
www.jensen-nmr.fr
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