Postdoc: The biophysics of chaperones and ribosomes, studied using optical tweezers and single-molecule fluorescence
We are recruiting for a new single-molecule biophysics position in which integrated optical tweezers and single-molecule fluorescence are central. Cells are thought to engage in a wide range of protein manipulations, in order to fold proteins and keep them functioning properly. However, which precise ‘actions’ are performed at the molecular level has remained obscure because of challenges in following the structure of proteins. Our lab has pioneered using optical tweezers to show how chaperones extend, clamp, confine, and processively pull on protein chains (Science 2007, Nature 2013, 2016, and 2020). It is a unique tool to manipulate single protein chains, and to “sense” how it folds up. In this project, you will integrate this technique with single-molecule fluorescence, which now allows us to directly visualize how other key proteins induce these crucial changes.
The project involves the design and execution of novel single-molecule experiments, developing new approaches to analyze the multi-dimensional and highly quantitative data, and to conceive underlying mechanistic models. From the many upcoming projects in our lab, you will be able to study several, both individually and together with other members of our team. Over the past years, we have been extending our approach to increasingly complex multi-protein systems, including molecular motors that translocate loops of protein chains, and entire ribosomes that synthesize protein chains and drive their folding and assembly. New results are making increasingly clear that ribosomes are far more extensive hubs of activity than previously thought; not just of polypeptide synthesis, but also for a wide spectrum of chaperone systems, the formation of multi-protein complexes during synthesis by multiple ribosomes, and interactions with RNA polymerases. With our single-molecule methods we have a unique opportunity to uncover how these dynamic and complex super-systems work. With collaborators, we study these same processes in cells. In particular, we make use of the DNA deep sequencing method selective ribosomal profiling, which shows which chaperones bind the ribosome during translation, at the genome-wide level. The combination of these techniques gives the opportunity to bridge the gap between single molecule events and functions within the cell.
About the group
We are looking for an outstanding experimental physicist or chemist with an interest in single-molecule techniques and a strong drive to excel in a competitive international environment.
Trained and graduated in a relevant field of research;
Post-doctoral research experience in a relevant field of research.
Terms of employment
The position is intended as full-time (40 hours / week, 12 months / year) appointment in the service of the Netherlands Foundation of Scientific Research Institutes (NWO-I) for the duration of two to three years. AMOLF assists any new postdoc with housing and visa applications and compensates their transport costs and furnishing expenses.
Group leader Biophysics
Phone: +31 (0)20-754 7100
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