Patrick Charbonneau, advisor
The complexity of protein-protein interactions enables proteins to self-assemble into a rich array of structures, such as virus capsids, amyloid fibers, amorphous aggregates, and protein crystals. While some of these assemblies form under biological conditions, protein crystals, which are crucial for obtaining protein structures from diffraction methods, do not typically form readily. Crystallizing proteins thus requires significant trial and error, limiting the number of structures that can be obtained and studied. Understanding how proteins interact with one another and with their environment would allow us to elucidate the physicochemical processes that lead to crystal formation and provide insight into other self-assembly phenomena. We explore this problem from a soft matter theory and simulation perspective.