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.
|Original language||English (US)|
|Number of pages||7|
|Journal||Organic and Biomolecular Chemistry|
|State||Published - 2016|
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Organic Chemistry