The Zhou group uses theory, computation, and experiment to address a range of topics in molecular and cellular biophysics.  Four main areas are: (1) thermodynamic and dynamic properties of phase-separated biomolecular condensates; (2) membrane association and binding kinetics of intrinsically disordered proteins; (3) structures and pathways of the self-assemblies of amyloid-β and other amyloidogenic proteins; and (4) functional mechanisms of glutamate-receptor ion channels.

Research Overview

SH3-PRM-BSA droplets
Phase-Separated Biomolecular Condensates
Inside cells, liquid-liquid phase separation leads to the formation of biomolecular condensates such as nucleoli, which mediate a myriad of cellular functions including ribosome biogenesis and transcription. The formation of biomolecular condensates is driven by one or a few proteins but regulated by numerous other macromolecular species. One focus of our studies is to elucidate the physical basis and macromolecular regulation of phase separation.
WASP-Cdc42 binding
Binding Kinetics (and Membrane Association) of Intrinsically Disordered Proteins
Proteins function by binding with a range of partners. 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 pathways. We are also studying the association of disordered proteins with a new class of partners, i.e., cell membranes.
Computation meets electrophysiology
Glutamate-Receptor Ion Channels
Ion channels are membrane proteins that allow ions to pass through cell membranes. Using molecular dynamics simulations, we are characterizing functional mechanisms of glutamate-receptor ion channels.
Nanofiber of RADA16
Amyloid-β Aggregation
Many proteins can spontaneously form β-strand rich aggregates (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 aggregates formed by amyloid-β and other amyloidogenic proteins.

News and Notable

  • Hot Publication Our work reporting extreme DNA compaction by protamine published in JACS

  • Grants The Zhou group is supported by grants from the National Institutes of Health.

Falling and Fusion of Protein Droplets

Under gravity, protein droplets fall and then fuse on a glass slide.  Macromolecular regulators can promote or suppress droplet formation as well as affect the material properties of the droplets. Read paper

Computer Cluster, Equipment, and Lab