Since the determination of the first protein structure in 1959, the prevailing dogma posited that the biological function of proteins is encoded in their three-dimensional structures; in short, a stable folded protein structure was thought to be a prerequisite for protein function. It is now evident that a large proportion of eukaryotic proteins (approximately 60 percent of proteins involved in cancer or cell signaling, for example) do not adopt well-defined three-dimensional structures, but are partly or entirely disordered. Such intrinsically disordered proteins perform critical functions in cellular signaling and regulatory mechanisms and are associated with debilitating human conditions that include cancer, neurodegenerative diseases, and amyloid diseases. Like all paradigm shifts, the generality and functional significance of intrinsically disordered proteins has taken some time to be recognized and accepted. However, the field has exploded in recent years as more and more intrinsically disordered proteins have been identified and their functional roles uncovered. There is now great interest in the physical and structural properties and biological function of intrinsically disordered proteins, and the study of these is a rapidly emerging field. Despite the recent surge of activity, the prevalence of protein disorder and its association with disease remains largely underappreciated. The goals of this symposium are to promote broader awareness of protein disorder and to catalyze new interest and activity in the field.