Optimization of SDD-AGE as a Method to Study Amyloid Conversion of Human Recombinant Prion Protein
Date
2014-08
Authors
Campbell, James
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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.
Description
Keywords
SDD-AGE, Prion, Amyloid, Prion, Amyloid
Citation
Campbell, 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 (Unpublished thesis).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.