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Issue 20, 2016
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Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions

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Abstract

We evaluate the ability of hexahistidine (His6) tags on peptide and protein substrates to recruit deoxyribozymes for modifying those substrates. For two different deoxyribozymes, one that creates tyrosine-RNA nucleopeptides and another that phosphorylates tyrosine side chains, we find substantial improvements in yield, kobs, and Km for peptide substrates due to recruiting by His6/Cu2+. However, the recruiting benefits of the histidine tag are not observed for larger protein substrates, likely because the tested deoxyribozymes either cannot access the target peptide segments or cannot function when these segments are presented in a structured protein context.

Graphical abstract: Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions

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Publication details

The article was received on 06 Apr 2016, accepted on 27 Apr 2016 and first published on 27 Apr 2016


Article type: Paper
DOI: 10.1039/C6OB00716C
Citation: Org. Biomol. Chem., 2016,14, 4697-4703
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    Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions

    C. Chu and S. K. Silverman, Org. Biomol. Chem., 2016, 14, 4697
    DOI: 10.1039/C6OB00716C

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