3-DIMENSIONAL MOLECULAR MODELING OF BOVINE CASEINS - ALPHA-S1-CASEIN

被引:75
作者
KUMOSINSKI, TF
BROWN, EM
FARRELL, HM
机构
[1] US Department of Agriculture, Eastern Regional Research Center, Agricultural Research Service, Philadelphia, Pennsylvania, 19118
关键词
CASEIN STRUCTURE; PROTEIN FUNCTIONALITY; MILK PROTEINS;
D O I
10.3168/jds.S0022-0302(91)78470-1
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
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 alpha-s1-casein was constructed using molecular modeling programs. The predicted structure of alpha-s1-casein contains a hydrophobic and a hydrophilic domain, which are connected by a segment of alpha-helix. This unrefined structure shows good agreement with global biochemical and chemical information concerning alpha-s1-caseins A, B, and C.
引用
收藏
页码:2889 / 2895
页数:7
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