PhD/Post-doc: Single Proteins at the Ribosome
Chaperones are central to protein biogenesis, but their action at the ribosome remains poorly understood. A central complication is the highly dynamic nature of this process, which involves polypeptide synthesis, folding, chaperone binding, and ATP cycles, as well as a possible interplay between chaperones. New tools now allow us to directly monitor these dynamics. 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). The recent integration of single-molecule fluorescence now allows us to visualise the composition of actively translating ribosome-chaperone-client complexes, pushing the envelope of technical possibilities. In this project, we use this novel approach together with ribosomal profiling in order to unravel the first steps of protein biogenesis in real time.
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