The human proteome contains a significant number of proteins that are (at least partially) intrinsically disordered. They show unusual structural features that enable them to participate in diverse cellular functions and play significant roles in cell signalling as well as in pathogenesis. For example, transcription factors contain a significant amount of disordered segments and the dynamics as well as coupling it with partner molecules are keys in the processes of recognition and many other cellular activities. Several neurodegenerative diseases (e.g., Alzheimer’s, Perkinson’s, Huntington etc.) and other amyloid diseases (including diabetes) are directly associated with the aggregation of one or more native proteins.

An aggregation-prone or amyloidogenic region in an intrinsically disordered protein sequence plays a crucial role in protein aggregation and amyloid formation. The residues in the amyloidogenic regions are high in sequence complexity and seldom overlap with low complexity regions, which are also largely abundant in disorder proteins.

Understanding the disordered proteins and proteome is useful for high-throughput functional annotation of proteins, drug target identification and drug discovery linking protein disorders. Come join us to know more on how Bioinformatics and Omics tools and techniques can be used to decipher the enigma of disordered proteins.