Postdoctoral positions on the intrinsically disordered proteins of the endocytic

Leibniz-Forschungsinstitut für Molekulare - via Softgarden - Berlin - 24-05-2022 zur Vakanz  

  • Berlin, Deutschland
  • With Professional Experience
  • 5/24/22

Postdoctoral positions on the intrinsically disordered proteins of the endocytic uptake machinery (f/m/d)

(Ref. 10/2022)

The Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) belongs to the „Forschungsverbund Berlin e. V. (FVB)“. The FVB is an institution of seven natural sciences research institutes in Berlin funded by the Federal Republic of Germany and the association of its federal states. The research institutes are members of the Leibniz association.

The Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) in Berlin is a non-university research institute that conducts basic research in molecular pharmacology and provides a vibrant and collaborative environment with state-of-the-art facilities for research and employees from all over the world.

We are looking for several
post-doctoral fellows
, funded amongst others by the ERC, to join the group
‘Integrated Structural Dynamics’
led by Dr. Sigrid Milles. The successful candidates will study the intrinsically disordered proteins involved in clathrin mediated endocytosis as well as their interplay with various interaction partners of the endocytic uptake machinery. The positions are to be filled

as soon as possible
and initially limited to
2 years
with the potential for extension.
The Milles lab (
https://www.leibniz-fmp.de/milles
) uses and develops integrated single molecule fluorescence and NMR spectroscopy approaches to study intrinsically disordered proteins with the aim of understanding the conformational dynamics regulating the early phases of clathrin mediated endocytosis, the major pathway for molecule import into the eukaryotic cell. The group is particularly interested to decipher and characterize the interactions at play and relate their characteristics to liquid-liquid phase separation as well as function within the cell.

Your profile:

We seek highly motivated, ambitious, and talented young scientists to join an enthusiastic and collaborative team in an outstanding scientific environment to perform research. The successful candidates should have a PhD in biophysics/biochemistry, a solid background in

NMR
or
(single molecule) fluorescence spectroscopy
as well as a strong interest in interdisciplinary work on protein dynamics. Candidates with a background in
cell biology
or
fluorescence imaging (microscopy)
are also encouraged to apply.

We offer:

  • An attractive environment in a pleasant, friendly working atmosphere with an excellent infrastructure
  • Employment with all benefits of the public service
  • Continuing education and training
  • Family service
Compensation is in accordance with the TVöD Bund (German public service) salary scale. Social benefits correspond to those of the public service.
We offer equal opportunities regardless of gender and welcome applications of disabled candidates. They will be preferred in case of equal qualification. We welcome applications from all backgrounds.

For more information please contact:

Dr. Sigrid Milles; e-mail:
milles@fmp-berlin.de

Homepage FMP:
http://www.fmp-berlin.de
On the FMP homepage please go to

Stellenangebote/Jobs

and click first on this advertisement and then on the button
“Online bewerben”
. Please combine your application documents including motivation letter, CV, contact information for three letters of reference and copies of degree certificates.

We are looking forward to your application!

Relevant publications:

Naudi-Fabra S, Tengo M, Jensen MR, Blackledge M, Milles S.
Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS.
J Am Chem Soc. 2021 Dec 8 ;143(48):20109-20121
Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M.
Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly.
Sci Adv. 2020 Apr 1 ;6(14):eaaz7095
Milles S, Jensen MR, Lazert C, Guseva S, Ivashchenko S, Communie G, Maurin D, Gerlier D, Ruigrok RWH, Blackledge M.
An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function
Sci Adv. 2018 Aug 22 ;4(8):eaat7778
Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M, Gräter F, Lemke EA.
Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors
Cell. 2015 Oct 22 ;163(3):734-45
Delaforge E, Milles S, Bouvignies G, Bouvier D, Boivin S, Salvi N, Maurin D, Martel A, Round A, Lemke EA, Jensen MR, Hart DJ, Blackledge M.
Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin α
J Am Chem Soc. 2015 Dec 9 ;137(48):15122-34.
Milles S, Lemke EA.
Mapping multivalency and differential affinities within large intrinsically disordered protein complexes with segmental motion analysis
Angew Chem Int Ed Engl. 2014 Jul 7 ;53(28):7364-7.
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