  Amyloid precursor with 770 amino acids dimerizes and aggregates, as do its c
terminal 99 amino acids and amyloid 40,42 amino acids fragments. The titled
question has been discussed extensively, and here it is addressed further using
thermodynamic scaling theory to analyze mutational trends in structural factors
and kinetics. Special attention is given to Family Alzheimer's Disease
mutations outside amyloid 42. The scaling analysis is connected to extensive
docking simulations which included membranes, thereby confirming their results
and extending them to Amyloid precursor.
