Termini capping of metal-poly-His peptide complexes induces the formation of α-helix
Author:
Affiliation:
1. Department of Chemistry
2. Ben-Gurion University of the Negev
3. Beer-Sheva 84105
4. Israel
5. Ilse Katz Institute for Nanoscale Science and Technology
6. Faculty of Chemistry
7. University of Wroclaw
8. 50-383 Wroclaw
9. Poland
Abstract
Capping of both N- and C-terminal induce α-helix formation in Cu2+-His6 peptide.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/RA/C5RA15385A
Reference37 articles.
1. Making the most of affinity tags
2. His-rich sequences – is plagiarism from nature a good idea?
3. The interaction of theEscherichia coliprotein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity
4. Specific poly-histidyl and poly-cysteil protein sites involved in Ni2+ homeostasis in Helicobacter pylori. Impact of Bi3+ ions on Ni2+ binding to proteins. Structural and thermodynamic aspects
5. Evolutionary Descent of Prion Genes from the ZIP Family of Metal Ion Transporters
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1. Zn(II) and Ni(II) complexes with poly-histidyl peptides derived from a snake venom;Inorganica Chimica Acta;2018-03
2. Poly-Xaa Sequences in Proteins - Biological Role and Interactions with Metal Ions: Chemical and Medical Aspects;Current Medicinal Chemistry;2018-01-22
3. Metal complexes of amino acids and peptides;AMINO ACIDS PEP PROT;2017
4. The unusual metal ion binding ability of histidyl tags and their mutated derivatives;Dalton Transactions;2016
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