Biophysical Society Thematic Meeting | Tutzing 2026

Single-Molecule FRET: The Next 30 Years

Wednesday Speaker Abstracts

PROBING THE RAPID INTERACTION DYNAMICS OF CHARGED DISORDERED PROTEINS Ben Schuler 1 ; 1 University of Zurich, Zurich, Switzerland 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 polyelectrolyte interactions but retain their disorder in the resulting complexes. Combining advanced single-molecule spectroscopy and other biophysical methods with concepts from polymer theory and molecular simulations can reveal the physical mechanisms underlying the dynamics, interactions, and phase separation of disordered proteins.

SPFRET/SMFRET - A STORY OF TOOLS MAKING (AND THEIR UTILIZATION) Shimon Weiss; Shimon Weiss 1 ; 1 UCLA, Los Angeles, CA, USA I will describe how and why spFRET/smFRET was developed and outline its evolution and refinement through the lens of transcription by RNA polymerase

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