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来自S-羧甲基角蛋白A的α-螺旋片段的氨基酸序列。统计分析。

Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Statistical analysis.

作者信息

Elleman T C, Crewther W G, Van Der Touw J

出版信息

Biochem J. 1978 Aug 1;173(2):387-91. doi: 10.1042/bj1730387.

Abstract

The distribution of the different types of amino acid residue within two helical segments isolated from the low-sulphur fraction of wool keratin was examined for periodicity and larger sequence repeats. Both were detected, the former corresponding to the geometry of the proposed coiled=coil structure and the latter suggesting a distant gene duplication, though the existence of the repeat might equally well be related to interactions within the microfibril.

摘要

对从羊毛角蛋白低硫组分中分离出的两个螺旋片段内不同类型氨基酸残基的分布进行了周期性和较大序列重复的检测。两者均被检测到,前者与所提出的卷曲螺旋结构的几何形状相对应,后者表明存在远距离基因重复,尽管这种重复的存在也可能同样与微原纤维内的相互作用有关。

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本文引用的文献

1
The structure of feather rachis keratin.羽毛羽轴角蛋白的结构
Proc Natl Acad Sci U S A. 1951 May;37(5):256-61. doi: 10.1073/pnas.37.5.256.
2
Is alpha-keratin a coiled coil?α-角蛋白是一种卷曲螺旋结构吗?
Nature. 1952 Nov 22;170(4334):882-3. doi: 10.1038/170882b0.
4
X-ray studies of crystalline proteins.结晶蛋白质的X射线研究。
Prog Biophys Mol Biol. 1969;19(1):1-132. doi: 10.1016/0079-6107(69)90003-0.

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