From alpha-helix to beta-sheet--a reversible metal ion induced peptide secondary structure switch

Org Biomol Chem. 2005 Jul 21;3(14):2500-2. doi: 10.1039/b505979h. Epub 2005 Jun 16.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Copper / chemistry*
  • Models, Biological*
  • Molecular Sequence Data
  • Multiprotein Complexes / chemistry
  • Peptides / chemistry*
  • Protein Structure, Secondary*
  • Zinc / chemistry*

Substances

  • Multiprotein Complexes
  • Peptides
  • Copper
  • Zinc