Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity

Author:

Wątły J.1234,Hecel A.1234,Wieczorek R.1234,Świątek-Kozłowska J.564,Kozłowski H.12345,Rowińska-Żyrek M.1234ORCID

Affiliation:

1. Faculty of Chemistry

2. University of Wroclaw

3. Wroclaw

4. Poland

5. Public Higher Medical Professional School in Opole

6. 45060 Opole

Abstract

Copper(ii) complexes with the studied His-rich motif are polymorphic, exhibit a 3–10 helix, and are more stable than a His6-tag complex.

Funder

Narodowe Centrum Nauki

Krajowy Naukowy Osrodek Wiodacy

Ministerstwo Nauki i Szkolnictwa Wyższego

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Reference41 articles.

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2. Snake venom metalloproteinases: Structure, function and relevance to the mammalian ADAM/ADAMTS family proteins

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4. J. W. Fox and S. M. T.Serrano , Snake Venom Metalloproteinases, A Handbook of Venoms and Toxins of Reptiles , CRC Press , Boca Raton, FL, USA , 2010 , pp. 95–113

5. N. R. Casewell , K.Sunagar , Z.Takacs , J. J.Calvete , T. N. W.Jackson and B. G.Fry , Snake venom metalloprotese enzymes , Oxford University Press , Oxford, UK , 2015 , pp. 347–363

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