Design and characterization of a homodimeric antiparallel coiled coil

被引：66

作者：

Gurnon, DG ^{[1
]}

Whitaker, JA ^{[1
]}

Oakley, MG ^{[1
]}

机构：

[1] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2003年 / 125卷 / 25期

关键词：

D O I：

10.1021/ja0357590

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications. Copyright © 2003 American Chemical Society.

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页码：7518 / 7519

页数：2

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