Alzheimer's disease, type II diabetes, Creutzfeldt–Jakob disease, and amyloid-related diseases: In each of these pathological situations, well-folded proteins undergo an irreversible transition from the “correctly folded” state to a collapsed β-sheet-rich structure. Here it is suggested that the aggregated form represents a global minimum in Gibbs energy for ensembles of protein molecules in general, and that at an infinite time any protein solution above a critical concentration will eventually undergo structural transition into the aggregated state.
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Ehud Gazit (2002) studied this question.