Context

Protein complexes underlie most biological functions, so that studying such complexes in native conditions (intact molecular species taken in solution) is of paramount importance in biology and medicine. Unfortunately, the two leading experimental techniques to date, X ray crystallography and cryo electron microscopy, involve aggressive sample reparation (sample crystallization and sample freezing in amorphous ice, respectively) which may damage the structures and/or create artifacts. These experimental constraints legitimate the use of mass spectrometry (MS) to study biomolecules and their complexes under native conditions, using electrospray ionization (ESI), a soft ionization technique developed by John Fenn (Nobel prize in chemistry, 2002). MS actually delivers information on the masses of the molecular species studied, from which further information on the stoichiometry, topology and contacts between subunits can be inferred. Thanks to ESI, MS is expected to play a pivotal role in biology to unravel the structure of macromolecular complexes underlying all major biological processes, in medicine and biotechnology to understand the complex patterns of molecules involved in pathways, and also in biotechnologies for quality checks.

Specific goals