Optimization of SDD-AGE as a Method to Study Amyloid Conversion of Human Recombinant Prion Protein
dc.contributor.advisor | Whitten, Steve | |
dc.contributor.author | Campbell, James | |
dc.contributor.committeeMember | Booth , Rachel | |
dc.contributor.committeeMember | Rudzinski, Walter | |
dc.date.accessioned | 2014-08-19T20:05:57Z | |
dc.date.available | 2014-08-19T20:05:57Z | |
dc.date.issued | 2014-08 | |
dc.description.abstract | Many 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.department | Chemistry and Biochemistry | |
dc.format | Text | |
dc.format.extent | 42 pages | |
dc.format.medium | 1 file (.pdf) | |
dc.identifier.citation | Campbell, J. (2014). Optimization of SDD-AGE as a method to study Amyloid conversion of human recombinant prion protein (Unpublished thesis). Texas State University, San Marcos, Texas. | |
dc.identifier.uri | https://hdl.handle.net/10877/5272 | |
dc.language.iso | en | |
dc.subject | SDD-AGE, Prion, Amyloid | |
dc.subject | Prion | |
dc.subject | Amyloid | |
dc.title | Optimization of SDD-AGE as a Method to Study Amyloid Conversion of Human Recombinant Prion Protein | |
dc.type | Thesis | |
thesis.degree.department | Chemistry and Biochemistry | |
thesis.degree.discipline | Biochemistry | |
thesis.degree.grantor | Texas State University | |
thesis.degree.level | Masters | |
thesis.degree.name | Master of Science |