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 Alzheimers 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.
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