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

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

Volume: 10 Issue: 1

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

Affiliation:

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

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.

Cite this article as:

Wada Kiyoko, Mizuno Toshihisa, Oku Jun-ichi and Tanaka Toshiki, ph-Induced Conformational Change in An A- Helical Coiled-Coil is Controlled by His Residues in the Hydrophobic Core, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408354