Molecular "tails" could play role in prion diseases

07/17/2013 | Chemical & Engineering News

Researchers looking at a 12-amino-acid section of human prion protein think they may have stumbled upon a structural anomaly -- tails on hexameric oligomers -- that could play a role in how misfolded prions influence nearby proteins, causing disease within and between species. The infectious forms of prions are believed to wreak havoc in neurological tissue, leading to bovine spongiform encephalopathy and other devastating diseases.

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