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Journal of Protein Chemistry

, Volume 13, Issue 8, pp 681–700 | Cite as

An energy-minimized casein submicelle working model

  • T. F. Kumosinski
  • Gregory King
  • H. M. FarrellJr.
Article

Abstract

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 ofκ-casein, fourαs1-casein, and fourβ-casein molecules. The models for the individual caseins were from previously reported energy-minimized, three-dimensional structures. Docking of oneκ-casein and fourαs1-casein molecules produced a framework structure through the interaction of two hydrophobic antiparallel sheets ofκ-casein with two small hydrophobic antiparallel sheets (residue 163–174) of two preformedαs1-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 fourαs1-caseins, while the central portion contains two hydrophbic cavities on either side of theκ-casein central structure. Symmetric and asymmetric preformed dimers ofβ-casein formed from the interactions of C-terminalβ-spiral regions as a hinge point could easily be docked into each of the two central cavities of theα-κ framework. This yielded two plausible energy-minimized, three-dimensional structures for submicellar casein, one with two symmetricβ-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.

Key words

Casein structure protien functionality milk proteins 

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Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • T. F. Kumosinski
    • 1
  • Gregory King
    • 1
  • H. M. FarrellJr.
    • 1
  1. 1.Eastern Regional Research CenterARS, USDAPhiladelphiaUSA

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