Controlling protein orientation at interfaces using histidine tags: an alternative to Ni/NTA.
A strategy for immobilizing histidine-tagged proteins at surfaces has been developed by using a macrocyclic chelator that enhances the stability and specificity of conventional histidine-tag technology and allows application of this technology to long-term studies including direct electrochemistry.
Johnson
Daniel L
DL
School of Chemistry, Monash University, Victoria 3800, Australia.
Martin
Lisandra L
LL
D002614:Chelating Agents / Q000737:chemistry; D004563:Electrochemistry; D004566:Electrodes; D006046:Gold / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry; D009571:Nitrilotriacetic Acid / Q000737:chemistry*; D010970:Plastocyanin / Q000737:chemistry*; D013254:Steroid 17-alpha-Hydroxylase / Q000737:chemistry*; D020349:Surface Plasmon Resonance; D013879:Thioredoxins / Q000737:chemistry*
D002614:Chelating Agents; D006639:Histidine; D013879:Thioredoxins; D006046:Gold; D009532:Nickel; D010970:Plastocyanin; D013254:Steroid 17-alpha-Hydroxylase; D009571:Nitrilotriacetic Acid