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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。II型片段的完整序列。

Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment.

作者信息

Crewther W G, Inglis A S, McKern N M

出版信息

Biochem J. 1978 Aug 1;173(2):365-71. doi: 10.1042/bj1730365.

Abstract
  1. The helical fragments obtained by partial chymotryptic digestion of S-carboxymethylkeratine-A, the low-sulphur fraction from wool, were fractionated into type-I and type-II helical segments in aqueous urea under conditions limiting carbamoylation. 2. The amino acid sequence of a 109-residue type-II segment was completed by using the sequenator. 3. When the data were incorporated into a helical model of 3.6 residues per turn the hydrophobic residues generated a band aligned at a slight angle to the helical axis. This result is in accord with the postulated coiled-coil structure of the crystalline regions of alpha-keratin.
摘要
  1. 通过对羊毛中的低硫组分S-羧甲基角蛋白-A进行部分胰凝乳蛋白酶消化得到的螺旋片段,在限制氨甲酰化的条件下,于尿素水溶液中被分离为I型和II型螺旋片段。2. 使用序列分析仪完成了一个109个残基的II型片段的氨基酸序列测定。3. 当将这些数据纳入每圈3.6个残基的螺旋模型时,疏水残基形成了一条与螺旋轴成小角度排列的带。这一结果与α-角蛋白晶体区域的假定卷曲螺旋结构一致。

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