We report surface plasmon resonance (spr) and confocal fluorescence results concerning the interaction of a gene-5-protein (g5p) with single-stranded DNA oligonucleotides (dT(25)) tethered to a gold surface. The spr data show that a highly stable g5p-ssDNA complex is readily formed on a gold surface with k(off) = 1.7 x 10(-3) s(-1). The extent of the complexion indicated involvement of the cooperative protein-protein interactions within the binding to DNA. In the experiments where dT(25) coexist with g5p in the solution, the fluorescence data show that g5p also mediates the binding between the non-complementary oligonucleotides in the solution and those immobilised on the surface. (C) 2012 Elsevier B. V. All rights reserved.