Conformation and Some Properties of Bovine α_s2-Group-casein

Alpha-Casein as a Molecular Chaperone

“…Biophysical characterisation of the purified S-casein proteins showed that the proteins possessed a similar degree of secondary structure to that expected from literature values [3,[35][36][37][38]. The far-UV CD spectra of purified S1-, S2-and S-casein proteins ( Figure 3) show a minimum at approximately 202 nm for S1-casein, 203 nm for S-casein and 205 nm for S2-casein and a second minimum for all three proteins at 222 nm.…”

Heat-induced Aggregation of Casein in Reconstituted Skimmed Milk at pH 3.30 – 3.55

“…Haga et al (1983) reported that α S2 -casein contained approximately 20% α-helix and a small amount of β-sheet, and that the content of the α-helix form in α S2 -casein was higher than that in α S1 -casein and β-casein. Under neutral conditions, heat treatment of α S2 -casein at 90℃ for 15 min causes destruction of approximately 35% of the α-helix, and the α S2 -casein solution becomes very turbid at >100℃ (Haga et al, 1983).…”