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Portal > Offres > Offre UMR5075-MAROND-005 - Post-doctorat en biologie structurale (H/F) : Intégrer la fluorescence à molécules uniques et la RMN pour l'analyse des protéines intrinsèquement désordonnées et leurs complexes

Post-doctoral position in structural biology (M/F) : Integration of single molecule FRET and NMR for the analysis of intrinsically disordered protein complexes

This offer is available in the following languages:
Français - Anglais

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General information

Reference : UMR5075-MAROND-005
Workplace : GRENOBLE
Date of publication : Monday, January 27, 2020
Type of Contract : FTC Scientist
Contract Period : 24 months
Expected date of employment : 1 September 2020
Proportion of work : Full time
Remuneration : According to the CNRS salary scale - minimum 2 617,05 €
Desired level of education : PhD
Experience required : Indifferent


A 2-year postdoctoral position funded by the ERC (StG MultiMotif) is available in the team of Sigrid Milles
at the Institut de Biologie Structurale. The team works on understanding the regulatory network built by
intrinsically disordered proteins of the endocytic uptake machinery using nuclear magnetic resonance
(NMR) and single molecule fluorescence spectroscopy.


Clathrin mediated endocytosis is the major pathway for molecule import into the cell and exerts
numerous vital functions, such as nutrient uptake or cellular signaling. Various proteins are involved in
this highly regulated uptake machinery, amongst those in particular adaptor proteins that contain long
intrinsically disordered regions (IDRs), i.e. regions without stable three-dimensional structure that interact
with other proteins from the endocytosis machinery. Although these interactions are crucial for
endocytosis, they are not very well understood due to the flexibility and dynamics of the protein
sequences they are embedded in, which makes them very difficult to study.

NMR and single molecule fluorescence count amongst the techniques that are best suited to study
intrinsically disordered proteins (IDPs). While NMR parameters inform about local structural propensities
of the IDP, single molecule fluorescence approaches, in particular Förster resonance energy transfer
(FRET/smFRET) can specifically probe long-range (up to ~ 10 nm). Together, the two techniques allow
assessing increasingly complex dynamic protein systems, such as those comprising the IDPs in

Goal of this postdoctoral project is to develop integrated NMR/single molecule fluorescence approaches
to address protein conformational dynamics. On the example of selected protein systems of the endocytic
pathway, the candidate will integrate fluorescence and NMR parameters using various types of single
molecule fluorescence and NMR experiments.


The successful candidate should have a PhD in biophysics/biochemistry, a solid background in NMR or
fluorescence spectroscopy/microscopy as well as a strong interest in interdisciplinary work on protein
dynamics. The candidate should feel comfortable doing experimental spectroscopic work as well as data
analysis and be interested in fluorescence instrumentation as the team develops its own single molecule
fluorescence spectrometer. Experience in instrumentation is not required, but would be a plus. Skills in
molecular biology and biochemistry are an advantage. Good scientific English is required.

Work Context

The Institut de Biologie Structurale (IBS, is situated on the EPN
science campus in Grenoble, in proximity to the ESRF (European Synchrotron Radiation Facility), the EMBL
(European Molecular Biology Laboratory) and the ILL (Institute Laue-Langevin). The IBS provides access to
an NMR facility (hosting 3 x 600, 700, 850 and 950 MHz spectrometers) and the single molecule
fluorescence equipment is developed within the team. Facilities for molecular biology, biochemistry and
cell biology are available and the IBS shares access to various research platforms via the ISBG (Integrated
Structural Biology Grenoble,

Constraints and risks

- product risks
- biohazards
- radiation risk (laser)

Additional Information

Details on the research of the team are available under

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