From alpha-helix to beta-sheet--a reversible metal ion induced peptide secondary structure switch.
Here we introduce a peptide model based on an alpha-helical coiled coil peptide, providing a simple system which can be used for a systematic study of the impact of different metal ions in different oxidation states on peptide secondary structure on a molecular level; histidine residues were incorporated into the heptad repeat to generate possible complexation sites for Cu2+ and Zn2+ ions.
Pagel
Kevin
K
Freie Universität Berlin, Institut für Chemie, Organische Chemie, Takustrasse 3, 14195 Berlin, Germany.
Vagt
Toni
T
Kohajda
Tibor
T
Koksch
Beate
B
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D008954:Models, Biological; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D015032:Zinc / Q000737:chemistry*
D046912:Multiprotein Complexes; D010455:Peptides; D003300:Copper; D015032:Zinc