A theoretical study of zinc(II) interactions with amino acid models and peptide fragments

Bartosz Trzaskowski, Ludwik Adamowicz, Pierre A Deymier

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

Density functional theory calculations have been employed to study the interaction between the Zn2+ ion and some standard amino acid models. The highest affinities towards the Zn2+ ion are predicted for serine, cysteine, and histidine. Relatively high affinities are reported also for proline and glutamate/aspartate residues. It was found that the zinc complexes with cysteine adopt a tetrahedral conformation. Conversely, complexes with one or two histidine moieties remain in an octahedral geometry, while those with three or more histidine groups adopt a square-planar geometry.

Original languageEnglish (US)
Pages (from-to)133-137
Number of pages5
JournalJournal of Biological Inorganic Chemistry
Volume13
Issue number1
DOIs
StatePublished - 2008

Keywords

  • Amino acids
  • Density functional theory
  • Enzymes
  • Metallization
  • Zinc

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

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