Huan-Xiang Zhou Biophysics Group

Inside cells, liquid-liquid phase separation leads to the formation of membraneless organelles such as nucleoli, which mediate a myriad of cellular functions including ribosome biogenesis and transcription. The assembly of membraneless organelles is driven by one or a few proteins but regulated by numerous macromolecular species. One focus of our studies is to elucidate the physical basis of macromolecular regulation of phase separation.

Proteins function by binding with small molecules and macromolecular partners; these processes often are under kinetic control. Continuing a long-standing interest, we are elucidating the determinants for the binding kinetics of disordered proteins, and are using the knowledge to alter binding kinetics.

Ion channels are membrane proteins that allow ions to pass through cell membranes. Using molecular dynamics simulations, we are characterizing functional mechanisms of ion channels and other membrane proteins.

Many peptides can spontaneously form β-strand rich assemblies (including amyloid-β peptides, leading to Alzheimer’s disease). By combining solid-state NMR and other structural techniques with computational modeling, we are determining structural models and pathways for the assemblies formed by amyloid-β and other peptides.