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Journal of Dairy Science Vol. 76 No. 9 2507-2520
© 1993 by American Dairy Science Association ®
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Three-Dimensional Molecular Modeling of Bovine Caseins: A Refined, Energy-Minimized kappa-Casein Structure

T. F. Kumosinski 1, E. M. Brown 1, and H. M. Farrell Jr. 1

1 US Department of Agriculture, Eastern Regional Research Center, Agricultural Research Service, Philadelphia, PA

A refined three-dimensional molecular model of kappa-casein has been produced using energy minimization techniques and a Kollman force field on a previously reported predicted three-dimensional structure. This initial model was constructed via molecular modeling techniques from sequence-based secondary structural prediction algorithms. Both the initial and refined structures agreed with global secondary structure analysis from vibration spectroscopy. The refined structure contained many of the features of the initial model, including two sets of antiparallel ßsheet structures containing predominantly hydrophobic side chains, which could form interaction sites with alphas1-casein. Two types of energy-minimized dimer and tetramer models are presented: 1) using Cys as potential intermolecular disulfide binding sites and 2) using the two sheets as possible hydrophobic self-association sites, without Cys interactions. All structures yielded good stabilization energies and are in agreement with chemical, biochemical, and physical chemical results obtained for kappa-casein.

Key Words: casein structure • protein functionality • milk proteins

Submitted on September 30, 1992
Accepted on March 22, 1993




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