PhD/Post-doc: Chaperone-Mediated Protein Folding

Delft University of Technology
October 10 2017
Position Type
Full Time
Organization Type

Chaperones are central to protein folding, maintenance, and disease, but how and when they affect protein chains has 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 visualise 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.

The position is intended as a full-time appointment. The formal employment and main activities will take place at AMOLF in Amsterdam. The student will participate in the TU Delft graduate school, and the PhD degree will be granted at the TU Delft.

This job comes from a partnership with Science Magazine and Euraxess

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