[dnautics]

> naturally since any change makes them unable to duplicate.

That's not true.

Don't worry about alphafold. Even if it's a really good extrapolation engine (and not a really good interpolation engine) the amyloid fold is unusual enough that I doubt that alphafold can heuristically solve structures much less assess energetic or kinetic factors (which is not what it was designed to do). Note that I am an alphafold optimist and am on record here saying that I consider alphafold to have solved the basic protein folding problem. More to the point, we don't have many reliable solved structures of amyloid folds, it's clear that they are heterogeneous anyways, and iirc no one has bootstrapped an infectious prion in vitro, which means we don't know exactly what makes something infectious... We can make prion amyloid in vitro but it isn't infectious unless it was seeded by an infectious prion amyloid.