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.
I received my PhD in Chemistry from Indiana University in 2019, where I developed time-resolved methods in charge detection mass spectrometry to follow the formation of large biomolecular assemblies from milliseconds to hours. Following my PhD, I moved to Oxford as a Marie Curie Postdoctoral Fellow in Dame Carol Robinson’s laboratory to investigate protein assemblies involved in signaling at the membrane. In 2021, I became a Senior Research Associate in Dame Robinson’s laboratory in the Kavli Institute for Nanoscience Discovery.
