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• RReasons ffor quicker i k dimerization di i ti kinetics ki ti of f C208 ßß-CNs CN Greater mobility y of C-terminal segment g Easier access of SH function Hydrophobic interactions • The dimerization sites in C6- and C-208 ß-CNs • RELECSH(4)NVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDEL QDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGV • SKVKEAMAPKHKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMH • QPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDM PIQAFLLYQ • EPVLGPVRGPF PIIVCSH (208) The France-Egypt Year Of Science And Technology, 2010
Hydrophilic Hydrophilic-Hydrophilic Hydrophilic patterns of different β CNs Native β CN has distinct arrangement of hydrophilic (ψ) -hydrophobic(φ) fragments (ψ- φ). The dimeric β CNs are in some sense symmetrical C208 β CND (ψ - φ ~ φ - ψ) C4 β CND (φ - ψ ~ ψ - φ) The France-Egypt Year Of Science And Technology, 2010 "P "Palindromic" lid i"
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: SDS-PAGE of the dimerizing β casei
Page 19 and 20: Chhaperone-like activity ac (%) Cha
Page 21 and 22: Consequence of Cys incorporation on
Page 23 and 24: − Average IgE (ng/ml) 35 30 25 20
Page 25: Our INRA team Isabelle Bronnec Aynu

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