Abstract

Controlling the self-assembly of biological molecules to form defined or functional structures with a high degree of predictability is a central aim for soft matter science and biological physics. While this is possible for a variety of colloidal and nanoscale materials, it has been more difficult to achieve for proteins. In large part, this is due to the complex nature of the protein surface, which influences the assembly process. Understanding this complexity is essential to reveal the mechanisms underlying important processes such as protein crystallization, the pathogenesis of protein condensation diseases, the aggregation of proteins during industrial manufacture and the formation of protein based materials. Using phase diagrams for human gamma D-crystallin (a protein found in the human eye lens), I will show that both mutagenesis and chemical modification of the protein surface can have a dramatic impact on anisotropic protein-protein interactions and hence the phase behaviour of the protein.