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. 2010 Oct 27;85(2):818–827. doi: 10.1128/JVI.01738-10

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FIG. 4. — Binding of T-Ag OBD proteins to poly(dT) DNA measured by fluorescence anisotropy. (A) Sequence of the 24-nucleotide poly(dT) probe used in this study. (B) Measurement of the T-Ag OBD-poly(dT) interaction via fluorescent anisotropy. Binding isotherms were measured in triplicate with 15 nM single-stranded DNA probe and increasing concentrations of the wild-type T-Ag-OBD (○) or of the V150A (□), F151A (Δ), S152A (▿), R154A (), L156A (+), T199A (⋄), H201A (*), H203A (×), R204A (▴), N210A (▪), or K214A (•) mutant protein. Curves were obtained by a nonlinear regression and fitting to a one-binding-site equilibrium. Error bars are not visible on the graph as they are smaller than the size of the symbols. K_ds (dissociation constants) were not calculated for these binding curves because they are not saturated although the relative affinities may be compared.

Inline graphic — Binding of T-Ag OBD proteins to poly(dT) DNA measured by fluorescence anisotropy. (A) Sequence of the 24-nucleotide poly(dT) probe used in this study. (B) Measurement of the T-Ag OBD-poly(dT) interaction via fluorescent anisotropy. Binding isotherms were measured in triplicate with 15 nM single-stranded DNA probe and increasing concentrations of the wild-type T-Ag-OBD (○) or of the V150A (□), F151A (Δ), S152A (▿), R154A (), L156A (+), T199A (⋄), H201A (*), H203A (×), R204A (▴), N210A (▪), or K214A (•) mutant protein. Curves were obtained by a nonlinear regression and fitting to a one-binding-site equilibrium. Error bars are not visible on the graph as they are smaller than the size of the symbols. K_ds (dissociation constants) were not calculated for these binding curves because they are not saturated although the relative affinities may be compared.