Temporal and spatially structured protein-protein interaction networks, “protein interactomes”, are at the heart of essential biological reactions from metabolism to signaling to trafficking. Although most work in this area focuses on intracellular processes, proteins outside the cell that comprise the matrix also constitute a highly sophisticated interactome that is equally relevant in controlling cell fate and function. In our studies of collagen and synthetic collagen-like proteins, we are studying the importance of intermolecular forces such as hydrophobicity and electrostatics in driving self-assembly of nanoscale structures. Models for self-assembly are implemented in software for protein design and used to control structure and specificity of protein composite materials with applications in drug delivery, biomaterials and bio-energy production.
From: Rutgers University