Understanding and controlling protein self-assembly is important in a wide variety of biological and industrial processes, including the crystallization of proteins for structural studies, the formulation of protein therapeutics, the development of treatments for protein aggregation disorders and the development of novel nanomaterials. Detailed analysis of the role that sequence and structure play in governing protein interactions in self-associating systems for single- or multi-component protein systems is essential to aid the development of rational approaches to control the assembly behavior and to understand the biology of these proteins. My future research will focus on using established, and developing novel, biophysical methods to measure molecular interactions between one or more proteins prone to self-assemble and to define critical regions within these proteins that govern their interactions. I will also explore how varying the molecular interactions between these types of proteins through mutations and/or environmental changes can affect the properties of the resulting protein assemblies and alter their specificity for interacting with other proteins. These molecular insights will be used to aid in the understanding of biological problems that involve protein self-assembly, such as prion transmission barriers and the formation of biofilms, as well as industrial problems such as improving the stability of protein therapeutics and the programmed assembly of complex, functional nanostructures.