Our research interests are centered on how changes in protein conformation drive self-assembly into larger structures and the role of cofactors in tuning these assembly pathways. We now know that uniquely structured aggregates interact with specific cellular components, i.e. chaperones, to promote pathogenic syndromes. More generally, macromolecular assemblies play key roles in scaffolding, organization, and spatial and temporal regulation of multiple cellular processes. Amyloid assemblies could have either useful or pathogenic activities, depending on their conformation, and how they recruit binding to cellular factors. Revealing the structural and mechanistic basis for self-associating proteins in complex with other factors will have important implications for understanding the pathology of neurodegenerative diseases. Our lab focuses on three main areas:

1) Molecular recognition in tuning protein conformation

2) Method development in hybrid structural analysis of protein complexes

3) Design of molecular recognition