Prion Disease
Folding of prion protein investigated
Published in Medical Letter on the CDC and FDA, July 11th, 2004
"A detailed mechanistic or structural understanding of the misfolding events that render the normal cellular prion protein, PrPC, amyloidogenic and infectious has been elusive. Many groups have observed that, under certain conditions, PrPC has a tendency to form beta-strand-rich fibers," scientists writing in the journal Trends in Biochemical Sciences report.
"A recently published protocol for in vitro conversion of PrPC shows that the formation of intermolecular disulfide bonds between monomers of recombinant PrP might play a role in...
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