Casein hydrodynamic properties

Dalgleish, D. G., and Morris, E. R. (1988). Interactions between carrageenans and casein micelles electrophoretic and hydrodynamic properties of the particles. Food Hydrocoll. 4 311-320. 

In a dilute protein solution, the nano length scale or the molecular structure of protein molecules determines the thermodynamic equilibrium between protein-protein and protein-water interactions. The consequent surface and hydrodynamic properties of proteins are resulted from the proportion of hydrophobic, hydrophilic, and charged amino acid residues. For example, caseins could adopt a random coil structure due to their flexible structure as a result of phosphorylated serine residues caseins indeed lack the ordered structures of a-helix, 3-sheet, and 3-turn found in globular proteins. This gives rise to better multifunctionality of caseins over globular proteins. 

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