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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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Proteins can adopt a variety of intricate conformations, including native, unfolded, misfolded and aggregated forms. In the latter case, generally 10’s-1000’s of protein molecules bind together to form an aggregate structure that could be random and amorphous or highly specific and well-ordered, such as an amyloid fibril. Amyloid fibril formation of certain proteins is associated with disease, including Alzheimer’s, Parkinson’s, and ALS, wherein the aberrant misfolding and aggregation of a particular protein is central to pathogenesis. Prion protein is notorious for forming infectious amyloid-like species that cause transmissible spongiform encephalopathies, including BSE, CJD and Kuru. In other cases, proteins form amyloid fibrils as part of their natural functional role, forming so-called functional amyloid.
Given the correct conditions, potentially any protein can be induced to form amyloid-like fibrils, also called nanofibrils. Nanofibrils hold promise for applications ranging from biosensors, nanowires, cell scaffolding, and perhaps as food ingredients. Protein nanofibrils have a high aspect ratio (1000’s nm in length, 7-12 nm wide), strength, and surface charge profile that make them attractive for such applications. The mechanisms of protein aggregation must be better understood in order to prevent amyloid formation, in the case of disease-associated amyloid, or such that it can be controlled in the case of engineering functional nanofibrils.
