Secondary structure of bovine αS2-casein:: Theoretical and experimental approaches

被引：22

作者：

Hoagland, PD ^{[1
]}

Unruh, JJ ^{[1
]}

Wickham, ED ^{[1
]}

Farrell, HM ^{[1
]}

机构：

[1] USDA ARS, Eastern Reg Res Ctr, Wyndmoor, PA 19038 USA

来源：

JOURNAL OF DAIRY SCIENCE | 2001年 / 84卷 / 09期

关键词：

alpha(S2)-casein; Fourier Transform infrared; circular dichroism; secondary structure;

D O I：

10.3168/jds.S0022-0302(01)74636-X

中图分类号：

S8 [畜牧、动物医学、狩猎、蚕、蜂];

学科分类号：

0905 ;

摘要：

Circular dichroism and Fourier transform infrared spectroscopy of bovine alpha (S2)-casein both report a 24 to 32% content of alpha -helix. A consensus of sequence based predictions for alpha -helix suggests a Lys(77)-Gln(91) helix within the sequence (Ser(61)-Arg(125)). This motif is repeated at (Ser(143)-Leu(207)), and this region contains a longer Thr(145)-Leu(177) predicted alpha -helix. A short, seven member alpha -helix may also organize the N-terminal peptide that precedes the first phosphoserine [-Srp-](3) cluster. As was found for other caseins studied by these spectroscopic methods, a high degree of extended beta -sheet (similar to 30%) and turns (25 to 30%) are predicted for alpha (S2)-casein.

引用

页码：1944 / 1949

页数：6

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