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- W2017144764 abstract "Abstract 1. 1.|The effect of succinylation and acylation on the association and conformation of α s1 -casein B has been studied by ultracentrifugation, optical rotatory dispersion (ORD) and nuclear magnetic resonance (NMR) spectroscopy. 2. 2.|Succinylation prevented the association of α s1 -casein B due to the additional negative charge introduced. 3. 3.|Acetyl α s1 -casein formed an associating system similar to that of the unmodified protein. n -Hexanoyl, n -octanoyl and n -decanoyl derivatives associated strongly with increasing protein concentration and remained in an aggregated form in dilute solution. Propionyl and n -butyryl α s1 -caseins behaved in a fashion intermediate between the acetyl and n -hexanoyl derivatives. 4. 4.|The size of the aggregates produced by the acyl derivatives formed a series similar to that found with corresponding derivatives of β-casein A, with a maximum at the n -hexanoyl derivative. This was attributed to enhanced hydrophobic bonding with increasing n -alkyl chain length and to structural differences in the organisation of the associating units. 5. 5.|ORD studies showed small differences in secondary structure between derivatives. NMR spectra of derivatives containing long n -alkyl chains revealed side-chain interactions which were not present in the native molecule." @default.
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- W2017144764 date "1973-12-01" @default.
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- W2017144764 title "The effect of succinylation and acylation on the physicochemical properties of αs1-casein B" @default.
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- W2017144764 doi "https://doi.org/10.1016/0005-2795(73)90278-x" @default.
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