My research employs native mass spectrometry to (i) capture the interactions among proteins, ligands, lipids, and other effectors, and (ii) to define the compositional requirements for complex formation. I develop methods, instrumentation, and analysis pipelines in native top-down mass spectrometry, enabling selective fragmentation of intact protein complexes to resolve their precise molecular composition. A central focus of my work is understanding how proteoform diversity, such as sequence variations and post-translational modifications, shapes molecular interactions at membranes, and how these processes are altered in neurological disorders.