Protein complexes are dynamic entities that alter their composition according to the tissue type, the nature of the cell itself (e.g., normal vs. diseased), and the intracellular localization. Such variability in subunit composition creates unique functional properties, enabling the complex to respond and adapt to varying cellular conditions. These abilities may be highly developed, and subjected to sophisticated modes of regulation. Exposing this structural plasticity is an important step towards understanding biological functions, however, unrevealing this enormous diversity is not a simple task. To maximize the information that can be obtained by mass spectrometry we are developing new experimental and data analysis methods.
For example, we developed an MS-based approach that enables to expose the diversity of subunit variants that comprise protein complexes. In addition, we have developed a generic approach to investigate ligand-driven protein complexes and define their allosteric mechanisms of function. We also contributed to the means by which the ion-mobility mass spectrometry approach is used for studying protein assemblies with unknown structures. Moreover, we recently devised a rapid mixing device for real-time MS analysis of protein complexes. In line with our past achievements, we not only aim to push the methodological and technological abilities of the native MS approach but also to combine it with complementary technologies for a comprehensive investigation of macromolecular assemblies.