Single proteins and chaperones at the ribosome

Date posted September 14, 2017
Type Postdoc positions

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 visualize 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.

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.

Contact info Sander Tans
Group leader Biophysics
Phone: +31 (0)20-754 7100

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