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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

ph-Induced Conformational Change in An A- Helical Coiled-Coil is Controlled by His Residues in the Hydrophobic Core

Author(s): Kiyoko Wada, Toshihisa Mizuno, Jun-ichi Oku and Toshiki Tanaka

Volume 10, Issue 1, 2003

Page: [27 - 33] Pages: 7

DOI: 10.2174/0929866033408354

Price: $65

Abstract

An α-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 α-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.

Keywords: coiled-coil, de novo design, folding, helical structure, ph dependence


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