publication . Article . 2008

Molecular dynamics study of zinc binding to cysteines in a peptide mimic of the alcohol dehydrogenase structural zinc site

Erik G. Brandt; Mikko Hellgren; Tore Brinck; Tomas Bergman; Olle Edholm;
Open Access
  • Published: 12 Dec 2008
Abstract
The binding of zinc (Zn) ions to proteins is important for many cellular events. The theoretical and computational description of this binding (as well as that of other transition metals) is a challenging task. In this paper the binding of the Zn ion to four cysteine residues in the structural site of horse liver alcohol dehydrogenase (HLADH) is studied using a synthetic peptide mimic of this site. The study includes experimental measurements of binding constants, classical free energy calculations from molecular dynamics (MD) simulations and quantum mechanical (QM) electron structure calculations. The classical MD results account for interactions at the molecul...
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free text keywords: Zinc, chemistry.chemical_element, chemistry, Density functional theory, Stereochemistry, Binding site, Coordination number, Molecule, Binding energy, Covalent bond, Crystallography, Molecular dynamics
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