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Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
Institute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, Switzerland
These authors contributed equally to this work.
* Author to whom correspondence should be addressed.
Received: 16 October 2013; in revised form: 6 November 2013 / Accepted: 19 November 2013 / Published: 21 November 2013
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 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.
Keywords: plant metallothioneins; metal-thiolate cluster; backbone cyclization; flexibility reduction; NMR spectroscopy
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MDPI and ACS Style
Tarasava, K.; Johannsen, S.; Freisinger, E. Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1. Molecules 2013, 18, 14414-14429.
Tarasava K, Johannsen S, Freisinger E. Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1. Molecules. 2013; 18(11):14414-14429.
Tarasava, Katsiaryna; Johannsen, Silke; Freisinger, Eva. 2013. "Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1." Molecules 18, no. 11: 14414-14429.