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dc.contributor.advisorBenson, Stacy D.
dc.contributor.authorBeshirs, Julia Megan
dc.date.accessioned2014-03-14T21:53:34Z
dc.date.available2014-03-14T21:53:34Z
dc.date.issued2007-07-01
dc.identifier.urihttps://hdl.handle.net/11244/8076
dc.description.abstractOne purpose of this study was to crystallize the major capsid protein, P3, for Bam35, belonging to the Tectiviridae family. Diffraction data is needed to determine the structure of P3. The hope is that this structure can confirm Bam35's place in a double trimer viral lineage spanning all domains of life. The other focus was on the DNA packaging vertex of PRD1, Tectivirdae's type species. One of the four proteins comprising this vertex, P6, was focused on to crystallize. Further structures would have to be determined from this arena for comparison of the viral self components. The viral self is an explanation of how viruses can diverge, rather than converge, to share extremely similar structural aspects, but have vastly different genome sequences and host preferences. Being able to solve these structures will allow for the confirmation of the divergence theory and an affirmation of the double barrel trimer viral lineage.
dc.formatapplication/pdf
dc.languageen_US
dc.publisherOklahoma State University
dc.rightsCopyright is held by the author who has granted the Oklahoma State University Library the non-exclusive right to share this material in its institutional repository. Contact Digital Library Services at lib-dls@okstate.edu or 405-744-9161 for the permission policy on the use, reproduction or distribution of this material.
dc.titleViral Self Components of the Tectiviridae Family
dc.typetext
dc.contributor.committeeMemberMaterer, Nicholas
dc.contributor.committeeMemberEl Rassi, Ziad
osu.filenameBeshirs_okstate_0664M_2385.pdf
osu.collegeArts and Sciences
osu.accesstypeOpen Access
dc.description.departmentChemistry Department
dc.type.genreThesis
dc.subject.keywordsbacteriophage bam35
dc.subject.keywordsbacteriophage prd1
dc.subject.keywordsmajor coat protein
dc.subject.keywordsviral evolution
dc.subject.keywordspackaging vertex
dc.subject.keywordscrystallization


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