Week 4 – More about Prions and Alzheimer’s

Question 1

What is protein misfolding cycling amplification used to generate prion infectious particles?

Question 2

The prion protein with the same primary sequence can cause different types of prion disease how is this possible?

Question 3

How might miss folded from protein be toxic to cells?

Question 4

What pH can PrP-C form a beta-sheet rich intermediate?

Question 5

As many as six copper ions bind to the N-terminal half of the PrP, which amino acid anchors this binding?

Question 6

What proportion of dementia is caused by Alzheimer’s disease?

Question 7

There are two protein aggregates that are linked to Alzheimer’s disease, what are they and where are they found?

Question 8

What is the most common length of peptide found in amyloid placks?

Question 9

What length of amino acids is the longest form of the amyloid precursor protein (APP)?

Question 10

The gamma-secretaries is a macromolecular assembly, what protein at its centre causes the cleavage of the precursor proteins?

Question 11

Why was is important to use synthetic prions to support the prion hypothesis?

Question 12

How can different prion diseases be causes by PrP with the same sequence?

Answer 12

Fibres have a different morphology

Question 13

In TSEs what form and how is PrP neuro-toxic?

Answer 13

Oligomers

Question 14

What happens to PrP-C at pH 4?

Answer 14

Partially unfolds and forms an intermediate beta sheet