Research

Membrane Protein Structural Proteomics

We develop native-state structural proteomics strategies to investigate integral membrane proteins within their physiological lipid environments. Our work focuses on transmembrane domains, which remain challenging for conventional structural biology methods. By applying footprinting in membrane mimetics and in situ systems, we seek to elucidate membrane protein structure, dynamics, and disease-associated conformational changes.

Intrinsically Disordered Proteins

We investigate intrinsically disordered proteins (IDPs), with particular emphasis on Tau, to understand how conformational ensembles regulate function and pathology. Unlike folded proteins, IDPs exist as dynamic structural populations that are highly sensitive to environmental cues and binding partners. By integrating footprinting and multi-modal MS approaches, we aim to characterize structural heterogeneity, aggregation-prone regions, and disease-associated conformational shifts relevant to neurodegenerative disorders.

Footprinting in Drug Development

We apply chemical footprinting strategies to map ligand binding, conformational changes, and protein–protein interactions in native and near-physiological systems. These approaches enable residue-level resolution of drug-induced structural perturbations, including transient and dynamic states often inaccessible to traditional structural methods. By integrating footprinting with quantitative MS workflows, we aim to accelerate mechanistic drug discovery and facilitate rational therapeutic design.