Optimization of SDD-AGE as a Method to Study Amyloid Conversion of Human Recombinant Prion Protein

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dc.contributor.advisorWhitten, Steve
dc.contributor.authorCampbell, James
dc.contributor.committeeMemberBooth , Rachel
dc.contributor.committeeMemberRudzinski, Walter
dc.date.accessioned2014-08-19T20:05:57Z
dc.date.available2014-08-19T20:05:57Z
dc.date.issued2014-08
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.description.departmentChemistry and Biochemistry
dc.formatText
dc.format.extent42 pages
dc.format.medium1 file (.pdf)
dc.identifier.citationCampbell, J. (2014). <i>Optimization of SDD-AGE as a method to study Amyloid conversion of human recombinant prion protein</i> (Unpublished thesis). Texas State University, San Marcos, Texas.
dc.identifier.urihttps://hdl.handle.net/10877/5272
dc.language.isoen
dc.subjectSDD-AGE, Prion, Amyloid
dc.subjectPrion
dc.subjectAmyloid
dc.subject.lcshAmyloid beta-proteinen_US
dc.subject.lcshAmyloidosisen_US
dc.subject.lcshPrionsen_US
dc.subject.lcshRecombinant proteinsen_US
dc.titleOptimization of SDD-AGE as a Method to Study Amyloid Conversion of Human Recombinant Prion Protein
dc.typeThesis
thesis.degree.departmentChemistry and Biochemistry
thesis.degree.disciplineBiochemistry
thesis.degree.grantorTexas State University
thesis.degree.levelMasters
thesis.degree.nameMaster of Science

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