Alexandre Chenal

This project aims to describe the hydrodynamic and thermodynamic properties of the CyaA toxin and the conformational changes it undergoes during its translocation process across the lipid membranes of Bordetella pertussis (secretion) and of […]

We are interested in investigating the effects of molecular crowding, i.e., excluded volume effects, mimicking the effects of high concentrations of macromolecular solutes found in biological fluids on biochemical properties of proteins. In particular, […]

CyaA, a 1706 residue-long protein, is one of the major virulence factors produced by B. pertussis and plays an important role in the early stages of respiratory tract colonization. This toxin uses an original […]

Hydrogen Deuterium eXchange followed by Mass Spectrometry (HDX-MS) is a recognized biophysical tool in structural biology capable of probing protein/ligand interactions, conformational changes, and protein folding and dynamics. The use of improved HDX-MS workflows […]