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[α-超螺旋蛋白的建模。序列选择、合成及性质]

[Modeling of alpha-superhelical proteins. Selection of sequence, synthesis, and properties].

作者信息

Potekhin S A, Iatsuk O I, Medvedkin V N

出版信息

Biofizika. 1990 Mar-Apr;35(2):205-11.

PMID:2369592
Abstract

An analysis of the alpha-tropomyosin primary structure suggests a periodic sequence able to form an alpha-superhelical conformation. A repeating unit (the heptapeptide monomer) was obtained by sequential synthesis in solution using pentafluorophenyl esters of the N-protected amino acids. The polyheptapeptide (Glu-Lys-Lys-Leu-Glu-Glu-Ala)n with an average molecular weight 6500 has been synthesized by polymerization of the heptamer. It is shown that the polymer product forms a stable alpha-superhelix at acidic pH in water solution.

摘要

对α-原肌球蛋白一级结构的分析表明,其序列具有周期性,能够形成α-超螺旋构象。通过使用N-保护氨基酸的五氟苯基酯在溶液中进行顺序合成,获得了一个重复单元(七肽单体)。通过七聚体的聚合反应合成了平均分子量为6500的聚七肽(Glu-Lys-Lys-Leu-Glu-Glu-Ala)n。结果表明,该聚合物产物在水溶液的酸性pH条件下形成稳定的α-超螺旋。

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