Molecular Biophysics Seminar - Ben Schuler

Molecular BioPhysics Seminar Series

Probing the interaction dynamics of disordered proteins with single-molecule spectroscopy

Ben Schuler, University of Zurich

https://www.oden.utexas.edu/news-and-events/events/2151---Ben%20Schuler/ 

The functions of proteins have traditionally been linked to their folded structures, but 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 combining advanced single-molecule spectroscopy with molecular simulations and other biophysical methods can reveal the dynamics, interactions, and phase separation of disordered proteins.References:

Borgia et al. (2018) Extreme disorder in an ultrahigh-affinity protein complex. Nature 555, 61-66

Sottini et al. (2020) Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes. Nat. Commun. 11, 5736

Heidarsson et al. (2022) Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein. Nat. Chem. 14, 224-231

Galvanetto, Ivanović et al. (2023) Extreme dynamics in a biomolecular condensate. Nature 619, 876-883

Galvanetto et al. (2024) Material properties of biomolecular condensates emerge from nanoscale dynamics. Proc. Natl. Acad. Sci. USA 122, e2424135122