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dc.contributor.advisorPeti, Wolfgang
dc.contributor.authorCollins, Grant Logan
dc.creatorCollins, Grant Logan
dc.date.accessioned2018-10-17T02:39:02Z
dc.date.available2018-10-17T02:39:02Z
dc.date.issued2018
dc.identifier.urihttp://hdl.handle.net/10150/630329
dc.description.abstractProtein phosphatase 5 (PP5) is a serine/threonine phosphatase (PSP) that participates in the cellular response to stress, particularly DNA damage. While participation in this pathway is unique to PP5, the structure of the enzyme is very similar to other members of the PSP family. The similarity between these phosphatases makes designing specific inhibitors for any one member of the PSP family exceedingly difficult. It is with this end goal in mind that I have chosen to express and characterize the catalytic domain of PP5 (PP5c) in order to examine the protein for differences that would allow for drug design. This characterization focused on activity and stability through the of pNPP assays and differential scanning fluorimetry, respectively.. These assays were done with protein phosphatase 1 (PP1) as a comparison and it was found that PP5c is most stable under different buffer conditions and has a lower activity level than PP1.
dc.language.isoen
dc.publisherThe University of Arizona.
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
dc.titleEXPRESSION AND PURIFCATION OF PP5C FOR DRUG DESIGN
dc.typetext
dc.typeElectronic Thesis
thesis.degree.levelbachelors
thesis.degree.disciplineHonors College
thesis.degree.disciplineBiochemistry
thesis.degree.nameB.S.
refterms.dateFOA2018-10-17T02:39:02Z


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