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Your position Biomolecular dynamics, such as conformational changes, are the understudied link between biomolecular structure and function. Single-molecule FRET is an established technique, unique
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to function, and this process is tightly regulated by a network of chaperone proteins. At the heart of this network is Hsp90, a molecular chaperone essential for the folding and maturation of at least 20% of
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are causing major changes in the physical environment, which may in turn fundamentally alter the functioning of ecosystems. Alpine and arctic ecosystems have remained relatively natural so far, but
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quantum sensing techniques to probe these emergent states. The successful candidate will join a small, collaborative team and be involved in all stages of the research cycle: design and operation of
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function. Single-molecule FRET is an established technique, unique in its capacity to resolve nanometer small conformational changes within single biomolecules (proteins, DNA, RNA), without suffering from
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, teaching and administrative tasks. The position is funded for 4 years with an initial contract for 1 year. At the end of the first year, an assessment based on performance and a detailed research proposal is
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: design and operation of scanning probe instrumentation fabrication of van der Waals heterostructures transport, optical spectroscopy, and quantum sensing experiments data analysis, modeling, and scientific
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discipline Strong interest in experimental quantum science and nanotechnology Keen to gain hands-on experience in laboratory research Analytical thinking, motivation, and the ability to work both independently
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. Building on our published and unpublished work, the successful candidate will advance nanopore trapping in new directions using solid-state and biological nanopores to identify previously inaccessible
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100%, starting January 2026 (negotiable) Proteins must fold correctly to function, and this process is tightly regulated by a network of chaperone proteins. At the heart of this network is Hsp90, a