Spectroscopic identification of different types of copper centers generated in synthetic four-helix bundle proteins.

Abstract

Using a combined rational-combinatorial approach, stable copper binding sites were implemented in template-assembled synthetic four-helix bundle proteins constructed by three different helices with only 16 amino acid residues. These peptides include two histidines and one cysteine at positions appropriate for coordinating a copper ion. Sequence variations… (More)

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Cite this paper

@article{Schnepf2004SpectroscopicIO, title={Spectroscopic identification of different types of copper centers generated in synthetic four-helix bundle proteins.}, author={Robert Schnepf and Wolfgang Haehnel and Karl E Wieghardt and Peter Hildebrandt}, journal={Journal of the American Chemical Society}, year={2004}, volume={126 44}, pages={14389-99} }