Author

Michael Mayer

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#protein folding Open access Sep 2026

Characterization of Single Ribosomes and Virus Particles with Large-Diameter Perfringolysin O Nanopores

Existing biological nanopores are often too narrow to accommodate large proteins and biomolecular complexes in their native folded states, precluding the analysis of megadalton assemblies. Here, we report the self-assembly of the cholesterol-dependent cytolysin Perfringolysin O (PFO) into stable transmembrane nanopores...

Andela Vracar, Veneta Salyahetdinova, S. Balog et al. · bioRxiv · 0 citations

#protein folding Open access Sep 2026

Pneumolysin nanopores with a 20 nm diameter characterize the size and shape of individual Tau oligomers

The self-assembly of 35 ± 5 monomers of the pneumolysin (PLY) toxin into stable transmembrane pores with diameters of 20.2 ± 3.0 nm is reported, and excellent low noise characteristics in the context of nanopore-based resistive pulse recordings are reported.

Anasua Mukhopadhyay, Wachara Chanakul, Yu Larpin et al. · bioRxiv · 2 citations