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Molecules 2013, 18(11), 14414-14429; doi:10.3390/molecules181114414
Article

Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1

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Received: 16 October 2013; in revised form: 6 November 2013 / Accepted: 19 November 2013 / Published: 21 November 2013
(This article belongs to the Special Issue NMR of Proteins and Small Biomolecules)
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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 plant metallothioneins; metal-thiolate cluster; backbone cyclization; flexibility reduction; NMR spectroscopy
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

AMA Style

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.

Chicago/Turabian Style

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.


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