Barrett, The Honors College Thesis/Creative Project Collection
Barrett, The Honors College at Arizona State University proudly showcases the work of undergraduate honors students by sharing this collection exclusively with the ASU community.
Barrett accepts high performing, academically engaged undergraduate students and works with them in collaboration with all of the other academic units at Arizona State University. All Barrett students complete a thesis or creative project which is an opportunity to explore an intellectual interest and produce an original piece of scholarly research. The thesis or creative project is supervised and defended in front of a faculty committee. Students are able to engage with professors who are nationally recognized in their fields and committed to working with honors students. Completing a Barrett thesis or creative project is an opportunity for undergraduate honors students to contribute to the ASU academic community in a meaningful way.
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- All Subjects: Biochemistry
Description
Conducted in collaboration with the Arizona Coalition to End Sexual and Domestic Violence, this project was a pilot survey of representatives at sexual violence organizations in Arizona and a best practices review of sexual violence organizations. It was carried out with the purpose of enhancing ACESDV's knowledge about sexual violence organizations so that the coalition will be able to offer informed and individualized support to these organizations in Arizona as it begins to pursue its new mission of addressing sexual violence.
ContributorsHarrach, Meagan L. (Author) / Bodman, Denise (Thesis director) / Dumka, Larry (Committee member) / Barrett, The Honors College (Contributor) / T. Denny Sanford School of Social and Family Dynamics (Contributor) / School of International Letters and Cultures (Contributor)
Created2014-05
Description
The purpose of this study was to provide a foundation for a plan for evaluations of the impact of the Learning Center on elementary school children with respect to academic achievement and school-related behaviors. Exploratory pre- and posttest data were collected and analyzed and recommendations were provided for a broader evaluation plan to be used in the future. The experience from the exploratory evaluation, limitations and the recommendations in this study can be used by Chicanos Por La Causa to strengthen the Learning Center and thereby optimize the benefit to the children served within the San Marina residential community.
ContributorsLodhi, Osman Sultan (Author) / Roosa, Mark (Thesis director) / Dumka, Larry (Committee member) / Perez, Norma (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor) / Department of Psychology (Contributor)
Created2014-05
Description
Several different queer feminist zines, along with the author's experiences in queer feminist zine making, are examined using the lens of J. Jack Halberstam's The Queer Art of Failure. Particular attention is paid to zines' unique composition from a variety of unexpected sources, and their subsequent ability to act as counterhegemonic documents. Queer feminist zine makers' critical engagement with the concept of community is also discussed.
ContributorsPruett, Jessica Lynn (Author) / Switzer, Heather (Thesis director) / Dove-Viebahn, Aviva (Committee member) / Barrett, The Honors College (Contributor) / School of Social Transformation (Contributor) / Department of English (Contributor)
Created2014-05
Description
Protein AMPylation is a recently discovered and relatively unstudied post-translational modification (PTM). AMPylation has previously been shown to play an important role in metabolic regulation and host pathogenesis in bacteria, but the recent identification of potential AMPylators across many species in every domain of life has supported the possibility that AMPylation could be a more fundamental and physiologically significant regulatory PTM. For the first time, we characterized the auto-AMPylation capability of the human protein SOS1 through in vitro AMPylation experiments using full-length protein and whole-domain truncation mutants. We found that SOS1 can become AMPylated at a tyrosine residue possibly within the Cdc25 domain of the protein, the Dbl homology domain is vital for efficient auto-AMPylation activity, and the C-terminal proline-rich domain exhibits a complex regulatory function. The proline-rich domain alone also appears to be capable of catalyzing a separate, unidentified covalent self-modification using a fluorescent ATP analogue. Finally, SOS1 was shown to be capable of catalyzing the AMPylation of two endogenous human protein substrates: a ubiquitous, unidentified protein of ~49kDa and another breast-cancer specific, unidentified protein of ~28kDa.
ContributorsOber-Reynolds, Benjamin John (Author) / LaBaer, Joshua (Thesis director) / Borges, Chad (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor) / School of Life Sciences (Contributor)
Created2014-05
DescriptionAn analysis and informal ethnography of the participatory culture in Phoenix, Arizona that identifies itself as "geeky" or "nerdy." Conducted through numerous interviews and academic research, the project looks at this active community under the scope of personal choice and togetherness.
ContributorsHuskinson, Harmony (Author) / Facinelli, Diane (Thesis director) / Scott, Suzanne (Committee member) / Barrett, The Honors College (Contributor) / Walter Cronkite School of Journalism and Mass Communication (Contributor)
Created2014-05
Description
Photosynthesis is a critical process that fixes the carbon utilized in cellular respiration. In higher plants, the immutans gene codes for a protein that is both involved in carotenoid biosynthesis and plastoquinol oxidation (Carol et al 1999, Josse et al 2003). This plastoquinol terminal oxidase (PTOX) is of great interest in understanding electron flow in the plastoquinol pool. In order to characterize this PTOX, polyclonal antibodies were developed. Expression of Synechococcus WH8102 PTOX in E. coli provided a useful means to harvest the protein required for antibody production. Once developed, the antibody was tested for limit of concentration, effectiveness in whole cell lysate, and overall specificity. The antibody raised against PTOX was able to detect as low as 10 pg of PTOX in SDS-PAGE, and could detect PTOX extracted from lysed Synechococcus WH8102. The production of this antibody could determine the localization of the PTOX in Synechococcus.
ContributorsKhan, Mohammad Iqbal (Author) / Moore, Thomas (Thesis director) / Redding, Kevin (Committee member) / Roberson, Robert (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor) / School of Life Sciences (Contributor)
Created2014-05
Description
Quercetin 2,3-dioxygenase from Bacillus subtilis has been identified and characterized as the first known prokaryotic quercetinase. This enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin to the corresponding depside and carbon monoxide. The first quercetinase was characterized from a species of Aspergillus genus, and was found to contain one Cu2+ per subunit. For many years, it was thought that the B. subtilis quercetinase contained two Fe2+ ions per subunit; however, it has since been discovered that Mn2+ is a much more likely cofactor. Studies of overexpressed bacterial enzyme in E. coli indicated that this enzyme may be active with other metal ions (e.g. Co2+); however, the production of enzyme with full metal incorporation has only been possible with Mn2+. This study explores the notion that metal manipulation after translation, by partially unfolding the enzyme, chelating the metal ions, and then refolding the protein in the presence of an excess of divalent metal ions, could generate enzyme with full metal occupancy. The protocols presented here included testing for activity after incubating purified quercetinase with EDTA, DDTC, imidazole and GndHCl. It was found that the metal chelators had little to no effect on quercetinase activity. Imidazole did appear to inhibit the enzyme at concentrations in the millimolar range. In addition, the quercetinase was denatured in GndHCl at concentrations above 1 M. Recovering an active enzyme after partial or complete unfolding proved difficult, if not impossible.
ContributorsKrojanker, Elan Daniel (Author) / Francisco, Wilson (Thesis director) / Allen, James P. (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor)
Created2014-05