Core polymers of casein micelles

Waugh, David F.; Creamer, Lawrence K.; Slattery, Charles W.; Dresdner, George

doi:10.1021/bi00806a011

Cited by 114 publications

(63 citation statements)

References 47 publications

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“…as-Casein is a substantial element of the micellar framework. 19 ) If the micelles are destroyed, as-casein must shift to the soluble fraction. The soluble fraction at 4°C contained slightly more as-casein than that at 37°C (Table II, Fig.…”

Section: Discussionmentioning

confidence: 99%

Changes in the Protein Composition and Size Distribution of Bovine Casein Micelles Induced by Cooling

Ono¹,

Murayama²,

Kaketa³

et al. 1990

Agricultural and Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Changes in the Protein Composition and Size Distribution of Bovine Casein Micelles Induced by Cooling

Ono¹,

Murayama²,

Kaketa³

et al. 1990

Agricultural and Biological Chemistry

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“…The first model of the casein micelle was published by Waugh (1958). This was followed by a series of papers on the formation and properties of artificial casein micelles, e.g., Waugh (1961), Noble and Waugh (1965), Waugh and Noble (1965) and Waugh, Creamer, and Slattery (1970). These studies were reviewed by Waugh (1971), who elaborated on a model for the structure of casein submicelles and explained for his choice of the term ''micelle'' to describe the calcium phosphate-calcium caseinate particles in milk.…”

Section: Structure Of the Casein Micellementioning

confidence: 99%

The casein micelle: Historical aspects, current concepts and significance

Fox

Brodkorb

2008

International Dairy Journal

315

186

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“…As the interaction of/3-casein with the micelle is regarded as primarily hydrophobic (Holt, 1992;Rose, 1968;Waugh et al, 1970), it seemed plausible to dock two/3-caseins within each of the two larger hydrophobic quadrants of the refined synthetic submicelle structure which occur to the right and left of the "rider" (see Fig. 3B, C).…”

Section: Submicelle Structurementioning

confidence: 99%

An energy-minimized casein submicelle working model

1994

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To develop a molecular basis for structure-function relationships of the complex milk protein system, an energy-minimized, three-dimensional model of a casein submicelle was constructed consisting of kappa-casein, four alpha s1-casein, and four beta-casein molecules. The models for the individual caseins were from previously reported energy-minimized, three-dimensional structures. Docking of one kappa-casein and four alpha s1-casein molecules produced a framework structure through the interaction of two hydrophobic antiparallel sheets of kappa-casein with two small hydrophobic antiparallel sheets (residue 163-174) of two preformed alpha s1-casein dimers. The resulting structure is approximately spherically symmetric, with a loose packing density; its external portion is composed of the hydrophilic domains of the four alpha s1-caseins, while the central portion contains two hydrophbic cavities on either side of the kappa-casein central structure. Symmetric and asymmetric preformed dimers of beta-casein formed from the interactions of C-terminal beta-spiral regions as a hinge point could easily be docked into each of the two central cavities of the alpha-kappa framework. This yielded two plausible energy-minimized, three-dimensional structures for submicellar casein, one with two symmetric beta-casein dimers and one with two asymmetric dimers. These refined submicellar structures are in good agreement with biochemical, chemical, and solution structural information available for submicellar casein.

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Core polymers of casein micelles

Cited by 114 publications

References 47 publications

Changes in the Protein Composition and Size Distribution of Bovine Casein Micelles Induced by Cooling

Changes in the Protein Composition and Size Distribution of Bovine Casein Micelles Induced by Cooling

The casein micelle: Historical aspects, current concepts and significance

An energy-minimized casein submicelle working model

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