The Zhou group uses theory, computation, and experiment to address a range of topics in molecular and cellular biophysics.  Four main areas are: (1) liquid-liquid phase separation; (2) binding kinetics of intrinsically disordered proteins; (3) functional mechanisms of ion channels and other membrane proteins; and (4) self-assembly of peptides.

Research Overview

SH3-PRM-BSA droplets
Liquid-Liquid Phase Separation
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.
WASP-Cdc42 binding
Binding Kinetics of Intrinsically Disordered Proteins
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.
Computation meets electrophysiology
Ion Channels and Other Membrane Proteins
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.
Nanofiber of RADA16
Peptide Self-Assembly
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.

News and Notable

  • Hot Publication Alan's paper on fuzzy membrane association of a disordered protein published in JACS Au

  • 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