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Title:Binding, Thermodynamic and Structural Studies of High-Affinity T Cell Receptor-Peptide MHC Interactions
Author(s):Jones, Lindsay Lee Ann
Doctoral Committee Chair(s):Kranz, David M.
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Health Sciences, Immunology
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.
Issue Date:2008
Type:Text
Language:English
Description:140 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008.
URI:http://hdl.handle.net/2142/84856
Other Identifier(s):(MiAaPQ)AAI3337813
Date Available in IDEALS:2015-09-25
Date Deposited:2008


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