Protein phase separation and conformation
How do Intrinsically Disordered Proteins (IDPs) shape themselves upon phase separation, and partner binding?
Natural materials
The mussel plaque is a mechanically sturdy material under tension and wet-dry cycling. What is the role of its porosity?
Tough polymeric materials
Using the end-functionalized hydrophilic PEG as our base polymer and catecholates, which are synthetic mimics of the mussel plaque modified amino acid L-Dopa, we create simple, yet tough dry polymeric networks that contain covalent and metal-coordinationate bonds. Our focus is to optimize toughness and understand and evntually tune the mechanisms that control the toughness. Our vision is to make these materials recyclable and turn them from laboratory systems to real-world materials. Our latest endeavor is to adjust the chemistry to enable us to work with bio-sourced polymers and create real, sustainable materials.
Polymer, Peptide and Protein phase separation
We have been using quantitative phase contrast methods to measure with extreme accuracy and small volumes phase diagrams of polyelectrolytes, peptides and proteins.
Using synthetic or genetic modifications, we impose controlled variations so we can make quantitative observations.
We couple these macroscopic measurements to microscopic dynamics (FCS), SAXS, and single molecule methods to learn about the change of conformations of the molecules and their partners as the molecules experience dilute or increasingly crowded environments
Natural Materials
We work on the byssal adhesive plaque of marine mussels. Having shown that not all mussels have porous plaques, our current efforts involve relating the porosity, and by extension the ecology, to engineering (such as adhesive) properties of the plaques.
Measuring the mechanics in the nanoscale
Using the measured nanoscale 3D structure to make realistic models of adhesion incorporating porosity