title: A theoretical study of zinc(II) interactions with amino acid models and peptide fragments.
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.
authors.affiliation: Department of Chemistry, University of Arizona, 1306 E. University Blvd., Tucson, AZ 85721, USA. trzask@u.arizona.edu
authors.forename: Bartosz
authors.initials: B
authors.lastname: Trzaskowski
authors.forename: Ludwik
authors.initials: L
authors.lastname: Adamowicz
authors.forename: Pierre A
authors.initials: PA
authors.lastname: Deymier
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D015032:Zinc