Our research focuses on a class of proteins known as tandem-repeat proteins such as ankyrin, tetratricopeptide and leucine-rich repeats. These proteins function as scaffolds for protein-protein interactions (PPIs) in a diverse range of biological contexts and are frequently deregulated in human diseases, particularly cancer. Our group and others have shown that the simple modular one-dimensional architecture of tandem-repeat proteins gives them distinctive properties compared with globular proteins and makes it uniquely straightforward to map the energetics of their structures and to rationally redesign their stability and molecular recognition properties. We are interested in developing proteins, peptidomimetics and small molecules to modulate repeat protein PPIs for therapeutic benefit.