CeNS Center for NanoScience LMU Ludwig-Maximilians-Universität München
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Single Molecule Mechanics of Chaperones

Project: Single molecule methods allow to observe the conformational dynamics of individual molecules over extended time periods with subnm resolution. In our lab, we have developed high resolution optical tweezers that allow the manipulation of individual protein molecules. In this project, we like to use optical tweezers to study Hsp90, a molecular machine involved in protein folding and quality control. We will hold the Hsp90 molecule in an optical tweezers and study its conformational dynamics in dependence of nucleotides and co-chaperones.

Requirements: The project is placed at the interface between biophysics and biochemistry.  Ideally, the successful candidate will have  a background in experimental physics/biophysics or biochemistry and  should not be afraid of an interdisciplinary project and environment.

1. Jahn, M., Buchner, J., Hugel, T., and Rief, M. (2016). Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments. Proc Natl Acad Sci U S A: 113, 1232-1237.

2. Pelz, B., Zoldak, G., Zeller, F., Zacharias, M., and Rief, M. (2016). Subnanometre enzyme mechanics probed by single-molecule force spectroscopy. Nat Commun: 7, 10848.

3. Jahn, M., Rehn, A., Pelz, B., Hellenkamp, B., Richter, K., Rief, M., Buchner, J., and Hugel, T. (2014). The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function. Proc Natl Acad Sci U S A: 111, 17881-17886.

Link to Prof. Rief's webpage: bio.ph.tum.de/home/e22-prof-dr-rief/rief-home.html