'Intrinsically disordered proteins', York, UK
Up to half of all human proteins contain regions that are intrinsically disordered. Understanding these structures is important because intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under physiological conditions in vitro. This type of protein is highly abundant in nature and their functional repertoire complements the functions of ordered proteins.
Numerous IDPs are associated with human diseases, including cancer, cardiovascular disease, amyloidoses, neurodegenerative diseases, and diabetes. Overall, intriguing interconnections among intrinsic disorder, cell signaling, and human diseases suggest that protein conformational diseases may result not only from protein misfolding, but also from misidentification, miss-signaling, and unnatural or nonnative folding.
The conference will bring together scientists interested in IDPs. Session topics will include:
- new methods for studying intrinsically disordered proteins;
- intrinsic disorder disease;
- intrinsic disorder and functional regulation;
- protein-protein interactions and intrinsic disorder.For further information, please visit: here(opens in new window)