ccβ acetate is a 17-residue peptide that folds into a coiled-coil trimer at low temperatures and aggregates to form amyloid fibrils at high temperatures. ccβ acetate serves as a simple model system for investigating α-helix to β-sheet conformational transitions and template-mediated aggregation processes associated with prion and amyloidogenic diseases. ccβ acetate can be used in studies of prion diseases and Alzheimer's disease [1].
In Vitro, ccβ acetate forms a thermodynamically stable native-like coiled-coil α-helical structure at temperatures below 0.71 ε/KB, and transitions to a β-strand-rich structure at temperatures above 0.71 ε/KB[1].
References:
[1]. Ding F, et al. Direct observation of protein folding, aggregation, and a prion-like conformational conversion. The Journal of biological chemistry. 2005 Dec 02;280(48):40235-40.
In Vitro, ccβ acetate forms a thermodynamically stable native-like coiled-coil α-helical structure at temperatures below 0.71 ε/KB, and transitions to a β-strand-rich structure at temperatures above 0.71 ε/KB[1].
References:
[1]. Ding F, et al. Direct observation of protein folding, aggregation, and a prion-like conformational conversion. The Journal of biological chemistry. 2005 Dec 02;280(48):40235-40.