Project 13

Probing multiprotein assemblies with native mass spectrometry

Principle Investigator: Prof. Dr. Nina Morgner

Research Areas: Native Mass Spectrometry

Summary

The correct (self-)assembly of molecular machines is of vital importance to ensure proper function of these multiprotein complexes. Analysis of this process and the necessary requirements, which allow unperturbed assembly into a complex’s functional state, is challenging. Native mass spectrometry allows us to analyze such protein assemblies regarding their stoichiometries, potential interaction partners as well as the assembly process itself. It is ideally suited to capture even the dynamic aspects of such processes, including intermediate steps in heterogeneous systems in dependence of well controlled environments or time dependencies. We want to understand the architecture and assembly mechanisms of multi- subunit machineries and assemblies, in the light of dependence on individual factors, such as the presence of nucleotides or chaperones in their reaction space, assembly factors needed for the assembly of different modules of a complex or the binding of specific substrates. In vitro assembly steps have to be probed individually and then correlated with results gained from similar experiments in more native environment. Especially for membrane proteins, native environments are still challenging to handle for many methods – we as well aim to push the boundaries regarding usable membrane mimics for native MS towards intact cellular membranes.