Milk protein aggregation is central to the manufacture of many dairy products but studies of individual milk proteins reveal that these proteins can participate in several different aggregation pathways; with different physiochemical environments leading to diverse final protein structures that display varied properties. This talk will focus on the aggregation of kappa casein and the associated casein macro peptide generated by cleavage with rennet. Drawing on new and existing data it will contrast the structures formed in dairy products with other aggregates, known as amyloid fibrils and compare the methods used to characterize and image gels and networks formed from these proteins. A better understanding of the landscape of protein folding and misfolding for dairy proteins will not only open up opportunities for new products and textures but also help to ensure that these proteins promote health on digestion.