Ryan
Hauss
Sponsor: James Letts, Ph.D. Molecular & Cellular Bio The final stage of cellular respiration in Eukaryotes occurs in the inner mitochondrial membrane and involves the transfer of electrons through a series of four membrane protein complexes, known as complexes, I- IV. The energy from the electron transfer reactions is used to pump-protons across the membrane, creating a proton motive force that is used to generate ATP via complex V. Typically the respiratory complexes are studied in isolation after their removal from the membrane, which could alter their structure and give a less accurate representation of the true electron transport chain process. Thus, my objective was to make inverted membrane vesicles from native bacterial membranes, known as sub-bacterial particles (SBPs), to measure the activity of the respiratory complexes in their native membranes. The model organism used was Paracoccus denitrificans, an α- protobacterium a close relative to the protomitochondria, making it a good candite to serve as a mitochondrial model. To characterize their activity and determine the success of vesicle formation I measured oxygen consumption by the SBPs under various conditions. Respirometry results suggest the protocol was successful, but the complexes were poorly coupled to ATP synthesis by complex V. Further optimization is needed to form well coupled particles with protocol. Characterizing C-peptide and Serum Albumin Protein Aggregation Using Single-Molecule, Super-Resolution Fluorescence Microscopy
Abstract profile. Full document pending author claim.
Authors:
Ryan Hauss
Date Created:
Not specified
Course Title:
Professor:
Not specified
About Paper:
Protein aggregation is associated with over 25 diseases, including Alzheimer's disease, Parkinson's disease, and type 2 diabetes. Aggregation occurs when misfolded proteins "stick" to one another and accumulate into larger species such as fibers or amorphous aggregate species. Characterizing factors that influence protein aggregation is crucial for understanding these diseases. In our experiment, we examined the effect of copper ion concentration, pH, surfactants, and temperature on the aggregation of bovine serum albumin and C-peptide. Serum albumin is a protein found in the blood that regulates osmotic pressure as well as lipid and mineral transport processes. C- peptide, which is produced during the formation of insulin, appears to help prevent aggregation of insulin and perform hormone-like roles. We utilized single-molecule, super resolution fluorescence microscopy to characterize the structures of the protein aggregates at the nanoscale. In combination with thioflavin T and turbidity assays, we seek to build an understanding of these protein aggregates at the molecular level. Survival of Salmonella, Listeria Monocytogenes, and Generic E. coli in Fresh and Recirculated Nutrient Solutions Used in Hydroponic Systems Elaine He
Source:
UC Davis / Chemistry / 2025
Topics:
No topics listed
Co-authors:
Ryan Hauss