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dc.contributor.advisorWhitten, Steve
dc.contributor.authorCampbell, James
dc.date.accessioned2014-08-19T20:05:57Z
dc.date.available2014-08-19T20:05:57Z
dc.date.created2014-08
dc.date.issued2014-07-11
dc.date.submittedAugust 2014
dc.identifier.urihttps://digital.library.txstate.edu/handle/10877/5272
dc.description.abstractMany common diseases are caused by amyloid proteins. Amyloid structures are β sheet rich, protease resistant, and can form polydisperse insoluble fibers. Due to these properties, biochemical/biophysical studies of amyloid have been hampered. One technique that is able to study amyloid is Semi Detergent Denaturing Agarose Gel Electrophoresis (SDD-AGE)3. The work presented here shows the optimization of several parameters such as gel thickness, electrophoretic conditions, and capillary transfer method. Through this optimization of SDD-AGE we show that it can be used to 1) study a recombinant human amyloid system and 2) achieve a higher resolution than has been previously reported.
dc.formatText
dc.format.extent42 pages
dc.format.medium1 file (.pdf)
dc.language.isoen_US
dc.subjectSDD-AGE, Prion, Amyloid
dc.subjectPrion
dc.subjectAmyloid
dc.subject.lcshAmyloid beta-protein
dc.subject.lcshAmyloidosis
dc.subject.lcshPrions
dc.subject.lcshRecombinant proteins
dc.titleOptimization of SDD-AGE as a Method to Study Amyloid Conversion of Human Recombinant Prion Protein
txstate.documenttypeThesis
dc.contributor.committeeMemberBooth , Rachel
dc.contributor.committeeMemberRudzinski, Walter
thesis.degree.departmentChemistry and Biochemistry
thesis.degree.disciplineBiochemistry
thesis.degree.grantorTexas State University
thesis.degree.levelMasters
thesis.degree.nameMaster of Science
txstate.departmentChemistry and Biochemistry


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