The ability to maintain macromolecular complexes in the gas phase of the mass spectrometer has allowed us to develop novel approaches to study the assembly and dynamics of multimeric complexes. Examples include the assembly of a hexameric molecular chaperone complex from isolated monomeric proteins. By examining related molecules, we are able to demonstrate the exchange of dimeric subunits between assemblies and further to extract kinetic parameters directly for the solution phase dissociation and formation of complexes. This research prompted us to design novel mass spectrometry equipment optimised for the analysis of macromolecular complexes and capable of transmitting high mass/low charge particles. Very recently this instrument has been used to isolate individual charge states from a mammalian chaperone, α crystallin the major protein in the eye lens, revealing for the first time the precise population of each of the oligomers that constitute the polydispersed assembly. Moreover we were able to mimic the effects of ageing on the quaternary structure of this dynamic. Overall therefore our research contributes to understanding the properties of macromolecular complexes and prompts new avenues of research for the investigation of complex biological systems.