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Biochemistry, Biophysics, and Structural Biology Commons

Open Access. Powered by Scholars. Published by Universities.®

Molecular Biology

2009

Carroll College

Articles 1 - 4 of 4

Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Cloning Of A Rare Chronic Wasting Disease Prion Allele From Mule Deer, Martha Bankhead Apr 2009

Cloning Of A Rare Chronic Wasting Disease Prion Allele From Mule Deer, Martha Bankhead

Life and Environmental Sciences Undergraduate Theses

The prion protein is thought to be the causative agent for Chronic Wasting Disease in mule deer (Odocoileus hemionus). Prion protein polymorphisms at amino acid 225 cause three different allele product combinations: homozygous 225 serine/serine, heterozygous 225 serine/phenylalanine, and homozygous 225 phenylalanine/phenylalanine. The most common combination of allele products in clinically progressed CWD in O. hemionus is serine/serine at 225. The phenylalanine substitution is underrepresented in diseased animals. The goal of this project was to clone the very rare phenylalanine encoding prion allele for future study. The polymerase chain reaction (PCR) was used to amplify the ...


The Effect Of Protein Disulfide Isomerase (Pdi) On In Vitro Conversion Of Mule Deer Prion Proteins, Alexander Nixon Apr 2009

The Effect Of Protein Disulfide Isomerase (Pdi) On In Vitro Conversion Of Mule Deer Prion Proteins, Alexander Nixon

Life and Environmental Sciences Undergraduate Theses

The objective of this project was to study Chronic Wasting Disease (CWD), a form of spongiform encephalopathy native to animals in the family Cervidae. The infectious agent in CWD is a misfolded form of the prion protein (PrPSc), which has undergone conversion from the normal, cellular prion protein (PrPc). The prion protein contains a disulfide bond, and the current project examined whether disulfide bond rearrangement is involved in the misfolding process. Using Protein Disulfide Isomerase (PDI), an enzyme that accelerates disulfide rearrangement, the efficiency of prion protein misfolding was monitored. Two different sources of normal prion protein were used: deer ...


Developing A Method For In Vitro Conversion Of Recombinant Mule Deer Prion Protein, Andrew Peterson Apr 2009

Developing A Method For In Vitro Conversion Of Recombinant Mule Deer Prion Protein, Andrew Peterson

Life and Environmental Sciences Undergraduate Theses

Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) occurring in free-ranging and captive populations of deer and elk. CWD is thought to involve a misfolded protein called the prion protein. The misfolding SC mechanism remains unknown, but the conversion results from misfolded PrP contacting normal PrPc, and inducing a conformational change of PrPcto PrPsc. Previous studies have shown the normal cellular PrPc, isolated from mule deer brain, has the ability to misfold in vitro when incubated with misfolded PrPsc. Instead of using deer brain as a source of the normal cellular form of the prion protein, this project ...


The Effect Of Culture Medium Composition On The Localization Of Peroxisomal Membrane Proteins In Yeast, Maria Miller Apr 2009

The Effect Of Culture Medium Composition On The Localization Of Peroxisomal Membrane Proteins In Yeast, Maria Miller

Life and Environmental Sciences Undergraduate Theses

Formation and degradation of peroxisomes are not well understood, but their absence leads to serious consequences. In the study described in this thesis, 1 sought to (1) verify previous work indicating that switching from glucose-rich medium to lipid-rich medium induces peroxisome formation; (2) reveal that switching back from lipid-rich to glucose-rich medium induces peroxisome degradation; (3) test the hypothesis that Pex3p is a class II PMP that enters the peroxisome from the endoplasmic reticulum during de novo peroxisome formation; and (4) test the hypothesis that Pxalp is a class I PMP that enters the peroxisomal membrane from the cytosol. I ...