Abstract

Intrinsically Disordered Proteins (IDPs) are a subset of proteins of which part or all of their sequence is found in an unfolded, flexible state. IDPs have been seen to be involved in several disorders, such as cancer and neurodegenerative disease. These flexible, disordered, regions have a higher rate of evolvability than the structured areas around it. Using the p53/p63/p73 superfamily and the prion protein as model protein families, we use a bioinformatics approach to investigate the evolution of disordered regions. These families are known to have variation of disorder among species and/or duplicates. Phylogenetic trees are constructed for each gene family. Disorder predictions are made for each sequence within the family. The evolution of these predicted regions of disorder are then analyzed in context of the phylogenetic trees. Through this, we show where in time the disorder arises and how the disorder has evolved.