pH-induced conformational change in an α-helical coiled-coil is controlled by his residues in the hydrophobic core

被引：13

作者：

Wada, K ^{[1
]}

Mizuno, T ^{[1
]}

Oku, J ^{[1
]}

Tanaka, T ^{[1
]}

机构：

[1] Nagoya Inst Technol, Dept Appl Chem, Showa Ku, Nagoya, Aichi 4668555, Japan

来源：

PROTEIN AND PEPTIDE LETTERS | 2003年 / 10卷 / 01期

关键词：

coiled-coil; de novo design; folding; helical structure; pH dependence;

D O I：

10.2174/0929866033408354

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An a-helical coiled-coil structure is one of the basic structural units in proteins. Hydrophilic residues at the hydrophobic positions in the coiled-coil structure play important roles in structures and functions of natural proteins. We reported here a peptide that formed a triple stranded a-helical coiled-coil showing the pH-dependent structural change. The peptide was designed to have two His residues at the hydrophobic positions of the center of the coiled-coil structure. The peptide folded into a triple stranded coiled-coil at neutral pH, while it unfolded at acidic pH. This construct is useful to create a protein that the structure or function is controlled by pH.

引用

页码：27 / 33

页数：7

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