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There is now a CONTENT FREEZE for Mercury while we switch to a new platform. It began on Friday, March 10 at 6pm and will end on Wednesday, March 15 at noon. No new content can be created during this time, but all material in the system as of the beginning of the freeze will be migrated to the new platform, including users and groups. Functionally the new site is identical to the old one. webteam@gatech.edu
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Advisor:
Andreas S. Bommarius, Ph.D. (Georgia Institute of Technology)
Co-Advisors:
Sven H. Behrens, Ph.D. (Georgia Institute of Technology) Yury O. Chernoff, Ph.D. (Georgia Institute of Technology)
Committee:
M. G. Fin, Ph.D. (Georgia Institute of Technology)
Julie A. Champion, Ph.D. (Georgia Institute of Technology)
Studies on Amyloid Aggregation and Cross-Species Prion Transmission
Amyloids are an important class of proteins because of their involvement in a number of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease. Notably, these proteins have a tendency to acquire a stable alternate conformation rich in beta-sheets and associate with each other to form fibrous ordered aggregates. Due to their unique properties and involvement in a number of fatal diseases there is a lot of interest in studying this class of proteins. Another characteristic of amyloidogenic proteins is that a given protein may adopt many distinct conformations, known as “variants” or “strains”. Once formed, a strain is efficiently reproduced under the same conditions on addition of the same prion protein. On the other hand, cross species transmission of prions is less efficient due to a “species barrier” which prevents the transmission of the prion state between prion proteins from different species with divergent sequences. The molecular basis of prion transmission and mechanisms of prion strain formation are not yet fully understood.
