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Updated: May 5, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Solution structure of the circular γ-domain analog from the wheat metallothionein E(c)-1
Katsiaryna Tarasava1, Silke Johannsen, Eva Freisinger
1Institute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, Switzerland. freisinger@aci.uzh.ch.
Abstract:
The first cyclic analog of a metallothionein (MT) was prepared and analyzed by UV and (magnetic) circular dichroism spectroscopy, ESI-MS as well as NMR spectroscopy. Results reveal that the evaluated cyclic γ-E(c)-1 domain of the wheat MT E(c)-1 retains its ability to coordinate two Zn(II) or Cd(II) ions and adopts a three-dimensional structure that is highly similar to the one of the linear wild-type form. However, the reduced flexibility of the protein backbone facilitates structure solution significantly and results in a certain stabilization of metal binding to the protein.
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