The Biophysical & Protein Chemistry Group is a research group focused on understanding how proteins respond to their environments, fold, and aggregate. Its work examines how both binding and non-binding molecules influence protein stability and dynamics, including ligands, dyes, drugs, ionic-liquid co-solvents, glycosaminoglycans found in the extracellular matrix, and different glucose molecules. The group also investigates how these factors affect protein-folding pathways and their physical and thermodynamic properties, using a bottom-up approach that recreates aspects of cellular environments in vitro.

A further focus is transforming protein aggregation, often associated with disease, into a controlled process for creating functional biomaterials. Researchers study aggregation pathways, kinetics, intermediate states, and structural changes in lysozyme, BMP-2, proteins linked to neurodegenerative conditions, and other globular proteins. The resulting insights support the design of bioactive, mechanically stable hydrogels, scaffolds, injectable systems, and drug-delivery platforms. These research efforts are directed toward potential applications in tissue engineering and regenerative medicine. The group also shares its work through publications and provides information about its members, collaborators, and research opportunities.