Biophysical Society Thematic Meeting | Tutzing 2026

Single-Molecule FRET: The Next 30 Years

Poster Abstracts

71-POS Board 35 FOLLOWING THE DIMERISATION AND LOOP DYNAMICS OF VIRAL CAPSID PROTEINS BY SOLUTION AND IMMOBILIZED SINGLE MOLECULE FRET Leon Torben Westermann 1 ; Christian Rönnau 1 ; Verena Hirschfeld 1 ; Christian Hübner 1 ; 1 University of Luebeck, Institute of Physics, Lübeck, Germany The murine norovirus (MNV) and the rabbit haemorrhagic disease virus (RHDV) are used as model systems to better understand the viral lifecycle.Viral capsid-ligand interactions can be studied using P-domain proteins as a model system. The P-domain is a structural protein component of the viral capsid, located on its surface.This study investigates how different ligands affect the MNV and RHDVb P-domain dimerisation and loop dynamics using single molecule FRET solution experiments and FRET experiments on immobilised single molecules, alongside other biophysical methods. The findings provide insights into the dynamics of P domains during ligand binding, offering a deeper understanding of crucial conformational changes during the viral lifecycle.

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