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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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Prof. John Straub, Boston University
Role of Sequence and Membrane on Amyloid Precursor Protein Structure and Function
School Colloquia
Aggregation of proteins of known sequence is linked to a variety of neurodegenerative disorders. The amyloid β (Aβ) protein associated with Alzheimer's Disease (AD) is derived from cleavage of the 99 amino acid C-terminal fragment of Amyloid Precursor Protein (APP-C99) by γ-secretase. Certain familial mutations of APP-C99 have been shown to lead to altered production of Aβ protein and the early onset of AD. We describe simulation studies exploring the structure of APP-C99 in micelle and membrane environments. Our studies explore how changes in sequence and membrane composition (including the presence of cholesterol) influence (1) the structure of monomeric APP-C99 and (2) APP-C99 homodimer structure and stability. Comparison of simulation results with recent NMR studies of APP-C99 monomers and dimers in micelle and bicelle environments provide insight into how critical aspects of APP-C99 structure and dimerization correlate with secretase processing, an essential component of the Aβ protein aggregation pathway and AD.
For more information contact Prof. Rigoberto Hernandez (404-894-0594).
Website: John Straub
