Week 3 – Prion Structure and Replication Flashcards
What proportion of scrapie PrP contains beta sheet structure and why is IR-spectroscopy particularly useful for studying the secondary structure of amyloid fibrils?
In recombinant amyloid fibrils which residues contain beta-sheet, how has deuterated water been used to find this out?
Why is it difficult to determine the 3D atomic level structure of amyloid fibrils?
Are the hydrogen bonds in cross-beta fibres inter-molecular or intra-molecular?
Why might the structure of recombinant amyloids be different from the brain derived amyloids?
Why might the ends of fibrils induce miss-folding in the prion protein?
During prion infection what is replicating?
Kinetics of fibrils growth can be described by three stages, what are they?
The process of fibrils formation can be accelerated by adding what?
There are rare cases of inherited prion diseases what are they caused by and how many have been identified? Also, they cause three distinct disease pheno-types name them.
Give some examples of prion mutations that stabilise the scrapie PrP isoform.
What type of stabilizing forces with PrPC are lost in some inherited mutations?
In vivo, where does the PrP misfolding take place and how might miss-folding spread from cell to cell?
