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

Authors: Wada K.; Mizuno T.; Oku J-i.; Tanaka T.

Source: Protein and Peptide Letters, Volume 10, Number 1, February 2003 , pp. 27-33(7)

Publisher: Bentham Science Publishers

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Abstract:

An agr -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 agr -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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866033408354

Publication date: 2003-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.