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dc.contributor.advisorKyle Strode
dc.contributor.advisorRon Wilde
dc.contributor.advisorDan Gretch
dc.contributor.authorSwanson, Elizabeth
dc.date.accessioned2020-04-30T10:03:36Z
dc.date.available2020-04-30T10:03:36Z
dc.date.issued2008-04-01
dc.identifier.urihttps://scholars.carroll.edu/handle/20.500.12647/3218
dc.description.abstractHuman immunodeficiency virus nucleocapsid protein (HIV-1 NC) is known to have both structural and nucleic acid chaperone functions in the replication cycle of the retrovirus. As a nucleic acid chaperone, NC protein interacts with TAR RNA and TAR DNA structures during the minus-strand transfer step of reverse transcription. The aim of this study is to use single molecule florescence resonance energy transfer (SM-FRET) spectroscopy to study biotin-immobilized TAR DNA hairpins at various concentrations of NC protein. The resulting data will subsequently be used to determine whether cooperative binding occurs between the NC protein and the TAR DNA hairpins. The results of this study are inconclusive; however, refinement of the experimental technique may provide conclusive data regarding cooperative binding in NC protein-TAR DNA interactions.
dc.titleThe Use of SM-FRET Spectroscopy to Determine Whether Cooperative Binding is Involved in the Chaperone Function of HIV-1 Nucleocapsid Protein
dc.typethesis
carrollscholars.object.degreeBachelor's
carrollscholars.object.departmentLife & Environmental Sciences
carrollscholars.object.disciplinesImmunology of Infectious Disease; Immunopathology; Medical Molecular Biology; Molecular Biology; Molecular Genetics; Virology
carrollscholars.legacy.itemurlhttps://scholars.carroll.edu/lifesci_theses/476
carrollscholars.legacy.contextkey12566840
carrollscholars.object.seasonSpring
dc.date.embargo12/31/1899 0:00


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