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Importance of phosphoryl residues for chaperone acivities of ßß-CNs. CNs The hydrophilic segment of chaperones plays an essential role increasing solubilities of target proteins. The expressed in E. coli recombinant ß-CNs are not phosphorylated what decreases their amphiphilicity amphiphilicity. Amino acid Sequence of native ß-CN and the sites for phosphorylation Smaller polarity of hydrophilic domain is the reason for poorer chaperone p activities of the mutant ß-CNs. The France-Egypt Year Of Science And Technology, 2010
Consequence of Cys incorporation on chaperone-like chaperone like activities of ß-CN. Absence of cysteinyl residues, is one of the common features among different chaperone families. The C4 ß-CN and C208 ß-CN have cysteinyl residue in position 4 and 208, respectively. The ß-CNs containing cysteine showed almost similar chaperone-like activities ti iti as WT ßß-CN. CN Thus incorporation of cysteine has no significant consequence in chaperone chaperone-like like acti activity it of monomeric ßß-CN. CN The France-Egypt Year Of Science And Technology, 2010
Page 1 and 2: ENGINEERING OF DAIRY PROTEINS AND T
Page 3 and 4: Average composition of f cow milk i
Page 5 and 6: Caséine κ 169 aa 19037 Da 1 Chymo
Page 7 and 8: P P P P β casein MKVLILACLV ALALAR
Page 9 and 10: F I Trp 143 monomer λ ↑ °CC Int
Page 11 and 12: Same conditions as for DLS. λmmax
Page 13 and 14: SDS-PAGE of bovine β casein and mu
Page 15 and 16: SDS-PAGE of the dimerizing β casei
Page 17 and 18: Hydrophilic Hydrophilic-Hydrophilic
Page 19: Chhaperone-like activity ac (%) Cha
Page 23 and 24: − Average IgE (ng/ml) 35 30 25 20
Page 25: Our INRA team Isabelle Bronnec Aynu

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