A novel approach to the preparation of ultraflat Ni substrates suitable to scanning probe microscopy imaging of immobilized polyhistidine-tagged proteins has been devised. Exploiting freshly cleaved mica, Ni thermal evaporation followed by thermal annealing in vacuum, and the template stripping method, we have obtained Ni substrates with a rms roughness as low as 0.12 nm, which bind readily polyhistidine-tagged proteins, enabling molecular resolution imaging of isolated molecules as well as of molecular submonolayers. Protein sample exposure to imidazole causes removal of the adsorbates, confirming the involvement of the polyhistidine tail in protein surface immobilization. © 2008 American Chemical Society.
Ultraflat nickel substrates for scanning probe microscopy of polyhistidine-tagged proteins
Alessandrini Andrea;Alessandrini Andrea;Facci Paolo
2008
Abstract
A novel approach to the preparation of ultraflat Ni substrates suitable to scanning probe microscopy imaging of immobilized polyhistidine-tagged proteins has been devised. Exploiting freshly cleaved mica, Ni thermal evaporation followed by thermal annealing in vacuum, and the template stripping method, we have obtained Ni substrates with a rms roughness as low as 0.12 nm, which bind readily polyhistidine-tagged proteins, enabling molecular resolution imaging of isolated molecules as well as of molecular submonolayers. Protein sample exposure to imidazole causes removal of the adsorbates, confirming the involvement of the polyhistidine tail in protein surface immobilization. © 2008 American Chemical Society.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
