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Biophysical principles of chaperone function studied by NMR spectroscopy

A postdoctoral research position is available in the group of Sebastian Hiller at the Biozentrum of the University Basel. The Hiller group is generally interested in elucidating fundamental biophysical aspects of chaperone function. The postdoctoral research project will investigate how a specific chaperone system recognizes and interacts with its client proteins and how this relates to its biological function and context. Building on our strong expertise on various bacterial and human systems, we integrate advanced solution NMR spectroscopy with additional structural and biophysics methods towards an atomic resolution description of structure, function and dynamics. 

The Hiller lab features an enthusiastic work environment with excellent infrastructure and a strong national and international collaboration network. Our facilities for integrated structural biology include four NMR spectrometers in the range of 600–900 MHz, cryo-electron microscopy, high-throughput crystallization, a biophysics and a proteomics core facility. The Biozentrum Basel is a worldwide leading research institution that is part of the international, vibrant community of the Life Science hub Basel. The research position is funded for at least 2 years with very attractive salary and benefits. The position is available immediately until filled.

We are looking for a colleague that is highly motivated, scientifically independent and creative, has high expertise in solution NMR spectroscopy and/or chaperone biochemistry, and is glad to contribute to a team environment. Applications should include a summary of current and future research interest, CV, publication list, and contact information for two references. Please send applications and informal queries to: 

Prof. Sebastian Hiller
Biozentrum, University of Basel
Klingelbergstrasse 70
4056 Basel, Switzerland
http://www.biozentrum.unibas.ch/hiller/

Literature:

  • Burmann BM, Gerez JA, ..., Riek R, Hiller S. Regulation of α-Synuclein by chaperones in mammalian cells. Nature 577, 127–132 (2020).
  • Hiller S. Chaperone-bound clients: The importance of being dynamic. Trends Biochem. Sci. 44, 517–527 (2019).
  • He L, Hiller S. Common patterns in chaperone interactions with a native client protein. Angew. Chem. Int. Ed. 57, 5921–5924 (2018).
  • Morgado L, Burmann BM, Sharpe T, Mazur A, Hiller S. The dynamic dimer structure of the chaperone Trigger Factor. Nat. Comm. 8, 1992 (2017).
  • He L, Sharpe T, Mazur A, Hiller, S. A molecular mechanism of chaperone–client recognition, Sci. Adv. 2, e1601625 (2016).