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The high specificity of Ni-dependent binding of his-tagged proteins to nitriloacetic acid terminated self-assembled monolayers is demonstrated using surface plasmon resonance. Binding quantitatively reversible with imidazole. Interaction of immobilized proteins with secondary ligands from the fluid adphase is more efficient than with his-tagged proteins bound to carboxy-dextrane layers. Very elegant and flexible approach, similar to Kubalek (et al. J Struct Biol 1994, 113: 117.)
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A metal-chelating lipid is constructed for the binding and crystallization of water soluble proteins. Whereas in earlier work, functionalized lipids had to be synthesized for each application, this approach derives its attractiveness from its flexibility for the immobilization of various proteins with surface-exposed histidines.
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Pack DW, Chen GH, Maloney KM, Chen C-T, Arnold FH. A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines. J Am Chem Soc. 119:1997;2479-2487 A metal-chelating lipid is constructed for the binding and crystallization of water soluble proteins. Whereas in earlier work, functionalized lipids had to be synthesized for each application, this approach derives its attractiveness from its flexibility for the immobilization of various proteins with surface-exposed histidines.
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