pH-induced conformational change in an alpha-helical coiled-coil is controlled by His residues in the hydrophobic
Kiyoko Wada1, Toshihisa Mizuno, Jun-Ichi Oku
1Department of Applied Chemistry, Nagoya Institute of Technology, Gokiso-cho, Showaku, Nagoya 466-8555, Japan.
Abstract:
An alpha-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 alpha-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.
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