University of Zürich, Schweitz
Professor Schuler’s laboratory investigates the structure and dynamics of proteins with cutting-edge single-molecule spectroscopy. He has made key contributions to our understanding of intrinsically disordered proteins (IDPs), proteins interacting with molecular chaperones, protein misfolding, as well as the behavior of proteins inside live cells. A key goal of his work is to reach mechanistic understanding based on quantitative physical models.
The cellular functions of proteins have traditionally been linked directly to their well-defined three-dimensional structures. It is becoming increasingly clear, however, that many proteins perform their functions without being folded. Single-molecule spectroscopy provides new opportunities for investigating the structure and dynamics of such “intrinsically disordered proteins” (IDPs). The combination of single-molecule Förster resonance energy transfer (FRET) with nanosecond correlation spectroscopy, microfluidic mixing, and related methods can be used to probe intramolecular distance distributions, reconfiguration dynamics and interactions on a wide range of timescales, even in heterogeneous environments, including live cells.
Host: Sebastian Deindl
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