After getting a master's degree in physics and chemistry, Dr. Claire Lesieur switched to biochemistry and biophysics for her PhD. She worked on the pore-forming toxin aerolysin, her favorite example of protein fold plasticity: it starts as a soluble monomer and ends as a heptameric pore. Dr. Lesieur did a post doc on the oligomerization of the cholera toxin B into pentamers aimed at isolating assembly intermediates. The difficulty of producing such intermediates experimentally drove her to explore computational approaches. The idea was to identify the amino acids determinant for the oligomerization and to investigate how they conduct subunit association. Ultimately, one may hope that the molecular detail of the process will help in designing better inhibitors against pathological oligomers.