L. Tubiana

This study presents the first high-resolution single-molecule analysis of kDNA network topology using AFM and simulations, revealing heterogeneous structure and buckling behavior.

This study shows dynamic TopoII binding accelerates topological relaxation of DNA knots, independent of substrate length, by enhancing search efficiency through facilitated diffusion.

This study designs proteins with reduced amino acid alphabets, finding that 6 letters are optimal for folding and that binding with partners is unavoidable with smaller alphabets, suggesting aggregation drove the evolution of a larger alphabet.