2026-09-21T12:16:58Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/82463 2023-07-11 col_2142_5131 col_2142_11615 com_2142_5130 com_2142_9130 com_2142_8903

Wittrup, K. Dane Boder, Eric Thomas 2015-09-25T20:44:12Z 2015-09-25T20:44:12Z 10000-01-01 1999 1999 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. The results of these studies clearly demonstrate the robustness of the yeast surface display system for quantitatively optimizing recognition parameters of biological macromolecules. Made available in DSpace on 2015-09-25T20:44:12Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9921662.pdf: 6065958 bytes, checksum: 0d025821522b583ee26004152b20269d (MD5) Previous issue date: 1999 Embargo set by: Seth Robbins for item 83744 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 148 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999. http://hdl.handle.net/2142/82463 (MiAaPQ)AAI9921662 eng Biology, Molecular Molecular Engineering of a Single-Chain FV Antibody Fragment to Femtomolar Affinity text Chemical Engineering Chemical Engineering University of Illinois at Urbana-Champaign Dissertation Ph.D.