Three-Dimensional Molecular Modeling of Bovine Caseins: _s1-Casein

¹ US Department of Agriculture, Eastern Regional Research Center, Agricultural Research Service, 600 East Mermaid Lane, Philadelphia, PA 19118

Structures derived from X-ray crystallography are extremely important in elucidating functional relationships for many proteins. However, the caseins of bovine milk are one class of noncrystallizable proteins. The complete primary and partial secondary structures of these proteins are known, but homologous proteins of known crystallographic structure cannot be found. Therefore, sequence-based predictions of secondary structure were made and adjusted to conform with global secondary structures determined by Raman spectroscopy. With this information, a three-dimensional structure for _s1-casein was constructed using molecular modeling programs. The predicted structure of _s1-casein contains a hydrophobic and a hydrophilic domain, which are connected by a segment of -helix. This unrefined structure shows good agreement with global biochemical and chemical information concerning _s1-caseins A, B, and C.

Key Words: casein structure • protein functionality • milk proteins

Submitted on December 3, 1990
Accepted on February 19, 1991

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