Effect of surfaces and osmolytes in modulating peptide assembly
Seminar | January 29 | 4-5 p.m. | 120 Latimer Hall | Canceled
Intrinsically disordered peptides are a special class of proteins that do not fold to a unique three-dimensional shape. These proteins play important roles in the cell, from signaling to serving as structural scaffolds. Under pathological conditions, these proteins are capable of self-assembling into structures that are toxic to the cell, and a number of neurodegenerative diseases, such as Alzheimers disease and Parkinsons disease, are associated with this self-assembly process. In this talk, I will discuss the effect of surfaces and the osmolytes urea and TMAO in regulating the structure and assembly of intrinsically disordered peptides. I will focus on two model systems, the mussel foot protein implicated in underwater adhesion of mussels to rocks, and the Tau peptide implicated in Alzheimers Disease.
Light refreshments will be served at 3:50 at The Coffee Lab