We related spectroscopic measurements of protein folding at neutral or slightly acidic pH with teh conditions where amyloid fibrils start to grow. The conclusion that wild type protein starts fibrillation from a native-like intermediate - was obtained.
On the system of both stefins we compared various models for protein folding, among them the contact order and framework models. It has been proven that in the case of stefins no pure model holds but rather they fold as a combination of the two mechanisms.
In this review paper we described and sorted existing models for the mechanism of amyloid fibril formation, with stress on domain-swapping.