Germany Job Openings

Leibniz-Forschungsinstitut für Molekulare Pharmakologie

PhD student position on studying intrinsically disordered proteins by NMR and single molecule FRET (f/m/d)

Berlin

September 9, 2024

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 belong to 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 a Ph D candidate to join the group ‘Integrated Structural Dynamics’ led by Dr. Sigrid Milles. The successful candidate will study the conformational dynamics of intrinsically disordered proteins involved in circadian time keeping. The position is to be filled as soon as possible and initially limited to 3 years with the potential for extension. The position is an 65% position for doctoral research.
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 their conformational dynamics and interaction landscape and, thus, their way of function. Along with this, we are also interested to discover the molecular mechanisms of liquid-liquid phase separation.
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 biochemistry, biophysics or related background and a strong interest in interdisciplinary work on protein dynamics using both NMR and (single molecule) fluorescence spectroscopy.
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 (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.
Are you interested?
For further information please contact Dr. Sigrid Milles; e-mail: milles@fmp-berlin.de.
Homepage: leibniz-fmp.de/milles
How to apply:
On the FMP homepage please go to Stellenangebote/Jobsand click first on this advertisement and then “Apply online”.
Please submit your application including a concise statement of research interest, CV, copies of degree certificates and contact information for two letters of reference as soon as possible. Applications will be considered upon submission.
We are looking forward to your application!

Relevant publications:
Naudi-Fabra S, Elena-Real CA, Vedel IM, Tengo M, Motzny K, Jiang PL, Schmieder P, Liu F, Milles S.
An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis.
Nat Commun. 2024 Jul 13;15(1):5884. doi: 10.1038/s41467-024-50212-4.

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

Vedel IM, Papagiannoula A, Naudi-Fabra S, Milles S.
Nuclear magnetic resonance/single molecule fluorescence combinations to study dynamic protein systems.
Curr Opin Struct Biol. 2023 Oct;82:102659. doi: 10.1016/j.sbi.2023.102659. Epub 2023 Jul 25.

Naudi-Fabra S, Blackledge M, Milles S.
Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins.
Biomolecules. 2021 Dec 24;12(1):27. doi: 10.3390/biom12010027.

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