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Updated: Jun 21, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Influence of NH-Sgamma bonding interactions on the structure and dynamics of metallothioneins
Núria Romero-Isart1, Baldo Oliva, Milan Vasák
1Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland.
Abstract:
Mammalian metallothioneins ([Formula: see text]) show a clustered arrangement of the metal ions and a nonregular protein structure. The solution structures of Cd(3)-thiolate cluster containing beta-domain of mouse beta-MT-1 and rat beta-MT-2 show high structural similarities, but widely differing structure dynamics. Molecular dynamics simulations revealed a substantially increased number of NH-Sgamma hydrogen bonds in beta-MT-2, features likely responsible for the increased stability of the Cd(3)-thiolate cluster and the enfolding protein domain. Alterations in the NH-Sgamma hydrogen-bonding network may provide a rationale for the differences in dynamic properties encountered in the beta-domains of MT-1, -2, and -3 isoforms, believed to be essential for their different biological function.
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