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Binding affinities of enriched aptamer pools for 5 rounds of selection. Measurements for each round are based on background-subtracted fluorescence values from a bead-based binding assay, scaled to saturation intensity. Binding affinity against thrombin increased over four rounds of selection, from an apparent Kd of 0.361 nM in Round 1 to 0.0075 nM in Round 4, before plateauing in Round 5.
