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dc.contributor.advisorPrunuske, Amy
dc.contributor.authorGu, Lucas
dc.date.accessioned2014-01-17T22:42:35Z
dc.date.available2014-01-17T22:42:35Z
dc.date.issued2011
dc.identifier.urihttp://digital.library.wisc.edu/1793/67927
dc.description7 p.en
dc.description.abstractProtein folding is a complex process that is mediated in the cell by molecular chaperones. Errors in protein folding can lead to aggregation of rnisfolded proteins, causing diseases such as Alzheimer's disease and Parkinson's disease. Understanding the regulation and mechanism of action of chaperones could help us better understand how to treat these diseases. One of the major chaperones in fungi involved in the folding of nascent polypeptides is the Hsp70 protein Ssb (Pfund C. et al., 1998). There are two Ssb homologs, Ssbl and Ssb2. Ssbl and Ssb2 differ by only four amino acids. These differences have been maintained in many fungal species, suggesting they may be functionally important (Takuno S. et al., 2009). To test this, I created chimera constructs to determine whether the coding sequence or in the promoter sequence of the genes is responsible for difference in function.en
dc.language.isoen_USen
dc.subjectBiochemistryen
dc.titleFunctional differences between the yeast Hsp70 molecular chaperones Ssbl and Ssb2en
dc.typeThesisen
thesis.degree.disciplineBiochemistryen


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