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dc.contributor.advisorZhang, Xuewuen
dc.creatorCormier, Kevin Williamen
dc.date.accessioned2015-09-01T20:25:02Z
dc.date.available2015-09-01T20:25:02Z
dc.date.created2013-08
dc.date.issued2013-07-25
dc.date.submittedAugust 2013
dc.identifier.urihttp://hdl.handle.net/2152.5/1730
dc.description.abstractNature uses proteins to catalyze a wide range of chemical processes that control cellular signaling. One such enzyme is ERK2 which plays a role in the transmission of signals by catalyzing the phosphorylation of its substrates. The signaling pathway that it is a part of is important in the control of growth, cell survival and differentiation. As with other proteins, its function is intimately related to its structure, both its activity and selectivity for binding partners affected by its conformation. A mutant of ERK2, discovered in a human oral squamous cell carcinoma cell line, consists of a substitution of a lysine for a glutamic acid residue in the common docking domain (E320K). The effects of this mutation on the structure of ERK2 are examined along with the effect that the conformational change has on protein-protein interactions. Because of the essential role catalysts play in lowering the activation barriers of otherwise inaccessible reaction pathways, chemists have long looked to nature for inspiration. The functionalization of C–H bonds is one such area of research, where the coveted exploitation of readily available hydrocarbon feedstock is impeded by the stability of the bonds. In this search for potential catalysts, chemists have looked to the metals that act as co-factors for many enzymes. Vanadium, long thought to be at work in halogenation reactions taking place in marine environments, was found to selectively catalyze the oxidation of hydrocarbons at the benzylic position. Understanding the mechanism of a reaction can lead to insights into ways to better harness reactivity and selectivity, something that nature does quite efficiently. In studying the biosynthesis of pyrrole-imidazole alkaloids, a means to mimic nature’s method for the dimerization of oroidin was achieved and the product outcome controlled.en
dc.format.mimetypeapplication/pdfen
dc.language.isoenen
dc.subjectMAP Kinase Signaling Systemen
dc.subjectPyrrolesen
dc.subjectVanadiumen
dc.titleExploration of Chemical and Biochemical Mechanisms of Catalysisen
dc.typeThesisen
dc.date.updated2015-09-01T19:57:19Z
dc.type.materialTexten
thesis.degree.grantorUT Southwestern Medical Centeren
thesis.degree.departmentGraduate School of Biomedical Sciencesen
thesis.degree.nameDoctor of Philosophyen
thesis.degree.levelDoctoralen
thesis.degree.disciplineCell Regulationen
thesis.date.available2015-09-01
dc.contributor.committeeMemberGoldsmith, Elizabeth J.en
dc.contributor.committeeMemberTambar, Uttamen
dc.contributor.committeeMemberCobb, Melanie H.en
dc.identifier.oclc919526509


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