Exploiting the microphase separation of block copolymers is a facile method of synthesizing nanometer- sized structures. The interactions of recombinant proteins with block copolymer surfaces displaying nanoscale order could be used to investigate intercellular signaling and for creating arrays of nanoreactors for lab- on- a- chip applications. A block copolymer of norbornene and norbornenedicarboxylic acid ( NOR/ NORCOOH) was synthesized and its hydrophilic block loaded with metal ions. Protein binding ability was examined by exposing the metal-loaded copolymer film to histidine- tagged green fluorescent protein ( hisGFP), washing with detergent to remove nonspecifically bound protein, and measuring the surface fluorescence. Results showed that nickel ions on the copolymer surface had superior hisGFP binding ability to copper and iron. Further investigation comparing the binding of hisGFP and GFP lacking the histidine tag showed that the nickel templated block copolymer was binding only hisGFP. It was concluded that the chelation between nickel on the polymer surface and histidine groups on the protein is the only significant binding force in the hisGFP- copolymer system.