Abstract
The metal-induced assembly of a designed peptide-based rubredoxin model is described. The C16C19-GGY peptide has the sequence Ac-K(IEALEGK) 2(CEACEGK)(IEALEGK)GGY-amide in which the presence of the Cys–X–X–Cys metal binding domain of rubredoxin was used to place cysteine residues at the hydrophobic “a” and “d” positions upon formation of a homodimeric α-helical coiled-coil. Circular dichroism spectroscopy shows that the apopeptide exists as a random coil and assembles into a coiled-coil in the presence of Cd 2+. Metal binding is monitored by the appearance of a new LMCT band at 238 nm. UV–Vis titrations and SDS–PAGE experiments are used to show that this designed metalloprotein exists as a metal-bridged coiled-coil dimer.
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