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Kranz, David M. Jones, Lindsay Lee Ann 2015-09-25T22:28:13Z 2015-09-25T22:28:13Z 10000-01-01 2008 2008 Finally, in chapter 5, fluorescence spectroscopy was used in stability and binding studies of scTCRs. Urea denaturation analysis was used to show that scTCRs engineered in the yeast display system have similar stabilities as single chain antibody Fvs. The yeast display system was successful in determining a location for covlalent attachement of a fluorophore that did not disrupt the binding site. Labeled scTCRs were used in several steady state and time resolved analyses, and binding to an anti-TCR antibody was observed, indicating that fluorescence spectroscopy may be useful in future studies of TCR-pMHC binding interactions. Made available in DSpace on 2015-09-25T22:28:13Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3337813.pdf: 2250081 bytes, checksum: dec9a80ea3143d48bdd2a33bea06d467 (MD5) Previous issue date: 2008 Embargo set by: Seth Robbins for item 86137 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 140 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008. http://hdl.handle.net/2142/84856 (MiAaPQ)AAI3337813 eng Health Sciences, Immunology Binding, Thermodynamic and Structural Studies of High-Affinity T Cell Receptor-Peptide MHC Interactions text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.