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The results of these studies clearly demonstrate the robustness of the yeast surface display system for quantitatively optimizing recognition parameters of biological macromolecules.","abstract_html":"Mutants of anti-fluorescein scFv antibody 4-4-20 improved more than 1000-fold with respect to ligand dissociation kinetics and equilibrium binding affinity have been isolated from mutagenized libraries displayed on yeast and screened by flow cytometry. Analysis of the nature of mutations conferring binding improvements suggests a potentially general strategy for engineering scFv antibodies for high affinity binding to target ligands. 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