Abstract：

Qiuye Li received his B.S. from Department of Chemistry, Tsinghua University in 2013 and he is now a qualified Ph.D. candidate in Case Western Reserve University. His research interests focus on structure biology of prion protein. Prion protein (PrP) is a protein-only infectious pathogen in many neurodegeneration diseases. Normal PrP (cellular PrP, PrP^c) is a functional membrane anchored protein mainly consisting of three α-helices. In prion diseases, PrP^c undergoes conformational changes and form aggregates, PrP scrapie (PrP^Sc). PrP^Sc can convert PrP^c into PrP^Sc, making prion disease infectious. However, no molecular mechanism was reported to explain the infectivity difference, mainly because of lacking a high resolution structure of PrP^Sc. In previous studies, different structure models of PrP^Sc were proposed with the help of computational methods, low resolution structure was also provided based on experimental data. In this talk, he will review the advances in the study of PrP^Sc structure and propose several other biophysical methods to solve a high resolution structure of PrP^Sc.