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Interaction dynamics of disordered proteins: From disordered complexes to biomolecular phase separation

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If you have a question about this talk, please contact Ella de Csillery .

Many proteins perform essential functions without being folded. Quantifying the highly dynamic and conformationally diverse ensembles of these intrinsically disordered proteins (IDPs) and their interaction mechanisms is an important aspect of understanding their functions. A remarkable example are highly charged IDPs, which can form high-affinity interactions but retain their disorder in the complexes. I will illustrate how advanced single-molecule spectroscopy combined with molecular simulations and other biophysical methods can be used to probe the dynamics and interactions of such disordered systems, which range from 1:1 dimers and oligomers to phase-separated droplets.

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