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, Misfolding and Aggregation

Protein folding has often been described as the “second half of genetics” as 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 devastating diseases such as Alzheimer’s disease, Parkinson’s disease, Type II diabetes, and Prion disorders. Our research seeks to uncover the fundamental principles that govern protein folding, misfolding, and aggregation. Using novel chemical and optical probes, we study protein structure and conformational dynamics at high resolution to dissect the molecular events underlying these processes. We also explore how cofactors and cellular environments influence protein aggregation to unravel the underlying mechanisms of the formation of biological aggregates and their physiological and pathological consequences.

Self-Assembled Biomaterials

Many examples in nature show that filamentous protein aggregates exhibit unique properties that make them attractive as a versatile class of biomaterials. Our research also explores the rational design and development of novel nanobiomaterials through the controlled self-assembly of macromolecules, including proteins.