pH-induced conformational change in an alpha-helical coiled-coil is controlled by His residues in the hydrophobic core.
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.
Wada
Kiyoko
K
Department of Applied Chemistry, Nagoya Institute of Technology, Gokiso-cho, Showaku, Nagoya 466-8555, Japan.
Mizuno
Toshihisa
T
Oku
Jun-Ichi
J
Tanaka
Toshiki
T
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006639:Histidine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D014461:Ultracentrifugation / Q000379:methods
D010455:Peptides; D006639:Histidine