Document Type and Release Option
Thesis (restricted to Georgia Southern)
The relationship between the three dimensional structure between a protein or enzyme and their specific function is a well-known concept in biochemistry. Calcium and calcium binding proteins are classic examples of this relationship. These proteins often contain various EF hand sites and bind calcium differently at each site, influencing the protein’s interaction with cysteine proteases, also referred to as caspases. Caspases are enzymes responsible for the intracellular substrate degradation that occurs in the cell death process. Previous data has shown that when calcium is present and calcium binding proteins, such as calbindin-d28K interact with the caspases, apoptosis can be inhibited. Therefore, these proteins have implications in cancer treatments as well as various neurodegenerative diseases such as Huntington's Disease and Alzheimer's. Very little information exists in the current primary literature in regards to protein structure changes of the executioner caspases (3 and 7) or the initiator caspases (8 and 12) in the presence and absence of calcium ions. This study will first amplify and isolated large amounts of the caspases of interest via molecular biology techniques and then investigate the effects of calcium ions on the protein folding of caspase 3. Structural changes and binding interactions will be monitored using circular dichroism spectroscopy. Data from this project will lead to a better understanding of apoptosis and could provide more targets for treatment of cancers and neurodegenerative diseases.
Love, Lauren K., "Investigation of protein conformational changes as a signal for apoptosis" (2019). University Honors Program Theses. 437.