Seeing and sensing chaperone-mediated protein folding acceleration
Chaperones are central to protein folding, maintenance, and disease, but how and when they affect protein chains as remained difficult to study directly. Recently it has become possible to detect protein conformational changes mediated by chaperones, as we have shown at the single-molecule level using optical tweezers for SecB, Trigger Factor, and Hsp70 (Science 2007, Nature 2013, Nature 2016). A recent extension by integrating single-molecule fluorescence, now allows us to visualize the composition of dynamic chaperone-client complexes, and their effects on client states. In this project, we will apply this approach to determine the mechanisms underlying chaperone foldase action, for a range of other intriguing chaperone systems and protein clients.
About the group
You need to meet the requirements for a doctors-degree.
Terms of employment
The position is intended as full-time (40 hours / week, 12 months / year) appointment in the Netherlands Foundation of Scientific Research Institutes (NWO-I) for the duration of two years. AMOLF assists any new postdoc with housing and visa applications and compensates their transport costs.
Prof.dr.ir Sander Tans
Group leader Biophysics
Phone: +31 (0)20-754 7100
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