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. 



More information can be found on the group website: www.jensen-nmr.fr



Facilities

The Institute
for Structural Biology 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 (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 malene.jensen@ibs.fr. The Ph.D.
project will start in October 2026.



Recent publications of the group:


Kjaer et al. Nature
Commun. (2025)

Hierarchical folding-upon-binding of an intrinsically
disordered protein


Orand et al. Adv. Sci.
(2025)

Sequence- and docking-site-dependent contributions to multi-site
phosphorylation of an intrinsically disordered MAPK substrate


Orand et al. PNAS (2025)

Bipartite binding of the intrinsically disordered scaffold protein
JIP1 to the kinase JNK1

Mariño Pérez et al. Nature (2022).
Visualizing protein
breathing motions associated with aromatic ring flipping



Delaforge et al. J. Am. Chem. Soc. (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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