Effect of surfaces and osmolytes in modulating peptide assembly

Seminar | January 29 | 4-5 p.m. | 120 Latimer Hall | Canceled

 Joan-Emma Shea, Department of Chemistry and Biochemistry, UC Santa Barbara

 College of Chemistry

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 Alzheimer’s disease and Parkinson’s 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 Alzheimer’s Disease.

 Light refreshments will be served at 3:50 at The Coffee Lab

 seminarcoordinator-cchem@berkeley.edu, 510-643-0572