Abstract
The structure and stability of casein micelles are determined in large measure by the amino acid sequences of the constituent αS1-, β-, and κ- caseins. In this paper we review, and attempt to connect with sequence data where possible: (1) molecular weight, structure, and dissociation of casein micelles; (2) physical characteristics of monomelic caseins, especially the distribution of charged and hydrophobic residues and the possible occurrence of helical regions; and (3) forces involved in association of monomers.
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