4 Often, they play a crucial role in many life functions. 1 They are found in bacterial chaperones, 2 snake venoms 3 and human genome.
Introduction Nature has developed histidine rich proteins (HRPs) in many living organisms. Finally, the formation of an α-helical structure is observed in pHG and in one of the mutated derivatives, indicating the importance of the sequence in the poly-(His-Ala) tags. The Cu( II) binding ability in pHG (Ac-EDDH 9G-NH 2) is more efficient than in the mutated derivatives, although the number of imidazoles that bind to Cu( II) ions are similar. Our study presents the properties of metal ion binding-histidine tag complexes and their mutated derivatives. The studied novel peptides are analogues of the short protected fragment of the pHpG (EDDH 9GVG 10) peptide, which was found in the venom of Atheris squamigera. This work illustrates the first study of novel poly-(His–Ala) peptides that bind Cu( II) applying both experimental techniques and extensive computational tools. The purpose of this work is to shed light on the behavior of poly-His sequences in their interactions with metal ions. However, their exact role in the biological systems is not clear. These sequences are also found in nature and are often highly conserved across different species. Polyhistidine-tags are often used for the affinity purification of polyhistidine-tagged recombinant proteins.
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