Probing the Dynamics and Interaction Mechanisms of Intrinsically Disordered Proteins with Single-Molecule Spectroscopy
Ben Schuler from the University of Zürich (Switzerland) showcased how the combination of single-molecule FRET with nanosecond correlation spectroscopy, microfluidic mixing, and other methods can be used to probe the dynamics and interaction mechanisms of intrinsically disordered proteins (IDPs) over a wide range of timescales and in heterogeneous environments, including live cells.
What is the webinar about?
The functions of proteins have traditionally been linked to their well-defined three-dimensional, folded structures. It is now clear, however, that many proteins perform essential functions without being folded. Quantifying the highly dynamic and conformationally diverse ensembles of such unfolded or ‘intrinsically disordered’ proteins (IDPs) is an important aspect of understanding their functional mechanisms. Single-molecule spectroscopy is ideally suited for investigating these systems. I will illustrate how the combination of single-molecule Förster Resonance Energy Transfer (FRET) with nanosecond correlation spectroscopy, microfluidic mixing, and other methods can be used to probe the intra- and intermolecular distance distributions, reconfiguration dynamics, and interactions over a wide range of timescales, and in heterogeneous environments, including live cells.
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