Exploring the conformational roles of signal sequences: synthesis and conformational analysis of lambda receptor protein wild-type and mutant signal peptides.

Exploring the conformational roles of signal sequences: synthesis and conformational analysis of lambda receptor protein wild-type and mutant signal peptides.
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探索信号序列的构象作用:λ受体蛋白野生型和突变信号肽的合成和构象分析。

DOI:
10.1021/bi00309a001
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发表时间:
1984
期刊:
影响因子:
2.9
通讯作者:
Gierasch,LM
Gierasch,LM
中科院分区:
生物学3区
文献类型:
--
作者:
Briggs,MS;Gierasch,LM

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Martha S.Briggs和Lila M.Gierasch*摘要:从遗传学证据来看,大肠杆菌受体蛋白(lamb蛋白)的分泌似乎与其信号序列预测的采用a-螺旋构象的趋势有关[EMR,S.D.,&Silhavy,T.J.(1983)过程。娜塔莉。阿卡德。SCI。美国80,4599],我们通过合成野生型和突变型LamB蛋白的大部分信号序列并用圆二色谱分析它们的构象来检验这一假说。野生型信号序列包含一个7个残基的疏水区,两侧是一个脯氨酸和一个甘氨酸。Chou-Fasman规则预测该片段将采用非螺旋构象。一个
Martha S. Briggs and Lila M. Gierasch* abstract: Secretion of the Escherichia coli\receptor protein (LamB protein) appears from genetic evidence to be correlated with the predicted tendency of its signal sequence to adopt an a-helical conformation [Emr, S. D., & Silhavy, T. J.(1983) Proc. Natl. Acad. Sci. USA 80, 4599], We have tested this hypothesis by synthesizing major portions of signal sequences from the wild-type and mutantLamB proteinsand analyzing their conformations by circular dichroism. The wild-type signal sequence contains a seven-residue hydrophobic region flanked by a proline and a glycine. Chou-Fasman rules predict that this segment will adopt an-helical conformation. An