{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86768"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86768","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Directed Evolution of T Cell Receptor Antagonists","abstract":"In Chapter 4, further engineering of TCR stability mutants to produce increased affinity binding for SAg is described. An optimized TCR fragment (containing nine mutations) was isolated after mutagenesis and selection, and was found to have approximately 1000-fold improved affinity for SAg. A soluble form of the mutant was shown to completely and specifically inhibit T cell activity in vitro.","abstract_html":"In Chapter 4, further engineering of TCR stability mutants to produce increased affinity binding for SAg is described. An optimized TCR fragment (containing nine mutations) was isolated after mutagenesis and selection, and was found to have approximately 1000-fold improved affinity for SAg. 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