The Conformation of Casein in Aqueous Solution.

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Abstract
Examination of light scattering data for [alpha]-casein solutions at pH 6.5 in ionic strength 0.1 phosphate-NaCl buffer supported earlier light scattering findings in cacodylate buffer that certain casein components exist in solution in the form of a random coil. Hydrodynamic data taken from the literature were interpreted in terms of the Mandelkern and Flory model for an impenetrable effective hydrodynamic sphere and agreement between theory and results for casein was observed. The physical properties of casein were viewed in terms of its amino acid composition. The optical rotatory properties of whole casein solutions in pH 6.5 phosphate buffer and in 6.6 [image] urea and for [beta]-casein in pH 6.5 phosphate buffer were consistent with the view that the proteins were not helical in these solvents.

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