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Solution structure of the circular g-domain analog from the wheat metallothionein Ec-1

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Publication date 2013
Author Tarasava Katsiaryna, Johannsen Silke, Freisinger Eva,
Project A. Structures and properties of plant metallothioneins and related artificial proteins - B. Site specific modifications of larger nucleic acids
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Original article (peer-reviewed)

Journal Molecules
Volume (Issue) 18
Page(s) 14414 - 14429
Title of proceedings Molecules
DOI 10.3390/molecules181114414

Open Access

Type of Open Access Publisher (Gold Open Access)


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 g-Ec-1 domain of the wheat MT Ec-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.