Background/Significance:
Proteostasis refers to the maintenance of the complex network involving the control the abundance and folding of the proteome. Proteostasis, which alludes to both the terms “protein” and “homeostasis,” functions to maintain balance within a variety of regulatory systems, and most specifically with reference to the proper folding and degradation of proteins.5 Proteins are large, complex molecules, which play a crucial role in all living organisms. The process of folding a newly synthesized protein is prone to error. In protein folding, the polypeptide chain folds into complex structures that are stabilized by hydrogen bonds, ionic bonds, hydrophobic interactions, and other chemical bond interactions. Protein folding is rarely accomplished without chaperones, a class of proteins that play a central role in proper protein folding. Chaperones
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RNA interference (RNAi) is a form of down-regulation of gene expression. The RNAi method functions by taking apart the mRNA molecules that carry the genetic information of a particular gene from the DNA to the ribosomes. I will feed bacteria containing the L4440 plasmid vector, which contains cyn-11, my gene of interest, to c. elegan worms: a model organism used to study protein-folding diseases. The cyn-11 gene will effectively be knocked down. The variables I will be measuring are the speed of worm movement and the size and number of protein aggregates produced both in the presence and absence of the cyn-11 co-chaperone. I will use video and photograph technology to perform a motility assay of the c. elegan worms. As controls, I will use the YFP control to ensure that RNAi is functioning, the Hsp-1 control as a positive control to assess if proteostasis is affected by knocking out the Hsp70 chaperone, and lastly an empty vector, which when fed to the c. elegans will assess whether plasmid introduction itself is toxic to the