ABSTRACT
Amyloid-like fibrils of proteins not involved in any known conformational disease have been shown to exert toxicity. Protofibrils and even smaller oligomers were shown to be responsible for toxicity; illustrated by the case of amyloid-beta peptide. Progressive myoclonus epilepsy of Unverricht-Lundborg type is believed to result in majority of cases from diminished expression and protein activity of stefin B. Apparent contradiction may be understood if we compare proteins of the same structural class: all stefin B-like and all stefin A-like. To determine stability of the proteins, urea denaturation curves were measured and analysed by a two-state approximation. To see the propensity for amyloid-fibril formation, the proteins were dissolved at slightly acidic conditions, which promote fibril formation of recombinant protein.
