Binding, Thermodynamic and Structural Studies of High-Affinity T Cell Receptor-Peptide MHC Interactions
Jones, Lindsay Lee Ann
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https://hdl.handle.net/2142/84856
Description
Title
Binding, Thermodynamic and Structural Studies of High-Affinity T Cell Receptor-Peptide MHC Interactions
Author(s)
Jones, Lindsay Lee Ann
Issue Date
2008
Doctoral Committee Chair(s)
Kranz, David M.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Health Sciences, Immunology
Language
eng
Abstract
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.
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