Issue 13, 2013
From the journal:

Chemical Communications

Femtomolar Zn(ii) affinity of minimal zinc hook peptides – a promising small tag for protein engineering†

Tomasz Kochańczyk,a   Piotr Jakimowiczb  and  Artur Krężel*a  

* Corresponding authors

a Laboratory of Chemical Biology, University of Wrocław, ul. Tamka 2, 50-137 Wrocław, Poland
E-mail: krezel@biotech.uni.wroc.pl
Fax: +48 71 375 2608
Tel: +48 71 375 2765

b Department of Protein Biotechnology, Faculty of Biotechnology, University of Wrocław, ul. Tamka 2, 50-137 Wrocław, Poland

Abstract

The minimal zinc hook peptide of Rad50 and its alanine mutants form highly stable Zn(II) complexes. These peptides were successfully used as a small, efficient tag for reversible Zn(II)-mediated protein homodimerization. The high stability, its biological consequences and potential applications in protein engineering are discussed.

Graphical abstract: Femtomolar Zn(ii) affinity of minimal zinc hook peptides – a promising small tag for protein engineering

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Article information

DOI
https://doi.org/10.1039/C2CC38174E
Article type
Communication
Submitted
13 Nov 2012
Accepted
20 Dec 2012
First published
21 Dec 2012

Chem. Commun., 2013,49, 1312-1314

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Femtomolar Zn(II) affinity of minimal zinc hook peptides – a promising small tag for protein engineering

T. Kochańczyk, P. Jakimowicz and A. Krężel, Chem. Commun., 2013, 49, 1312 DOI: 10.1039/C2CC38174E

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