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University of Illinois at Urbana-Champaign
Binding, Thermodynamic and Structural Studies of High-Affinity T Cell Receptor-Peptide MHC Interactions
Abstract
dc:descriptionFinally, 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biochemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Jones, Lindsay Lee Ann
- Contributors dc:contributor
-
- Kranz, David M.
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI3337813
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84856