Abstract
The postsynaptic density, a key regulator of the molecular events of learning and memory is composed of an elaborate network of interacting proteins capable of dynamic reorganization. Despite our growing knowledge on specific proteins and their interactions, atomic-level details of its full three-dimensional structure and its rearrangements are still largely elusive. In this work we addressed the extent and possible role of intrinsic disorder in postsynaptic proteins in a detailed in silico analysis. Using a strict consensus of predicted intrinsic disorder and a number of other protein sets as controls, we show that postsynaptic proteins are particularly enriched in disordered segments. Although the number of interacting partner proteins is not exceptionally large, the estimated diversity of the combinations of putative complexes is high in postsynaptic proteins.