We are a biophysical and biochemical research group with the main interest in protein structure and dynamics, protein folding, misfolding and amyloidogenesis, macromolecule self-assembly, biomaterials, and biosensor.

Protein folding is often referred to as the second half of genetics since the ability of a nascent protein to attain its proper, functional three-dimensional structure is essential for cellular function and viability. Misfolding and amyloidogenesis of proteins have been implicated in a number of diseases including Alzheimer’s disease, Parkinson’s disease, Type II diabetes, and Prion disorders. One direction of our research is towards understanding the structure, function, and conformational dynamics of proteins to understand the basic principles that govern protein folding in the cellular environment and to explore the underlying mechanisms of amyloid diseases caused by protein misfolding and aggregation.

Numerous examples in nature show that filamentous protein aggregates possess unique characteristics for their attractive use as a class of biomaterials. We are also interested in the rational design and development of novel nanobiomaterials via controlled self-assembly of macromolecules including proteins.