In a recent rapid communication (see attached paper), using principles of pattern formation, we expose some simple stategies to reliably produce perfect long range order in self-assembling systems. Most self-assembling systems exhibit short ranged order. This imperfection is detrimental to several practical applications. It is almost always possible to produce perfect patterns in small domain sizes but self-assembly over a larger areal span results in defects.

A postdoctoral associate position at MIT is available immediately, focused on elucidating the fundamental material science concepts that control the formation, behavior and in particular mechanical failure and fracture of fibrous amyloid protein materials. Amyloids form pathogens in diseases (Alzheimer’s, Parkinson’s), play a role in defining the properties of spider silk, and are found in many natural adhesives. These beta-sheet rich protein structures constitute an intriguing class of protein materials that self-assemble at room temperature to form characteristic hierarchical nanostructures and fibers, which combine exceptional strength and sturdiness, elasticity with bioactivity and the ability to self-heal.