Conformational analysis of periodic polypeptides

Conformational analysis of periodic polypeptides
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周期性多肽的构象分析

DOI:
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发表时间:
1993
期刊:
影响因子:
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通讯作者:
A. Nakajima
A. Nakajima
中科院分区:
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文献类型:
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作者:
M. Oka;A. Nakajima

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利用ECEPP和构象最小化方法对由Ala-Pro重复序列组成的周期多肽,即聚(Ala-Pro)进行了理论构象分析。计算结果表明,γ-螺旋是聚(丙氨酸-丙氨酸)最稳定的螺旋构象,而且大多数稳定的螺旋构象是其他类型的γ-螺旋和β-螺旋,单位残基升高值较大。多聚(Ala-Pro)的构象偏好表明,重复的Ala-Pro序列是设计人工蛋白质杆状主干构象的合适的氨基酸序列。
SummaryTheoretical conformational analysis was carried out for a periodic polypeptide composed of the repetitive Ala-Pro sequence, i.e., poly(Ala-Pro) using ECEPP and the conformational minimization procedure. Calculated results showed that a γ-helix is the most stable helical conformation of poly(Ala-Pro), and also that most of the stable helical conformations are other types γ-helices and β-helices with large value of the rise per residue. Obtained conformational preference of poly(Ala-Pro) indicates that the repetitive Ala-Pro sequence is a suitable amino-acid sequence for designing the rod-like backbone conformations of artificial proteins.
碱性富含脯氨酸的蛋白质的 13 个氨基酸的 N 端结构域对于储存在分泌颗粒中是必需的,并有助于从内质网中排出。
DOI: --
发表时间: 1992
期刊: The Journal of biological chemistry
影响因子: --
作者:
Castle,AM;Stahl,LE;Castle,JD
通讯作者: Castle,JD