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 caspases and calcium binding proteins with or without the addition of metal ions. This study will present preliminary results of the secondary structure conformational changes of BSA, capase-3, caspase-7, and caspase-9 upon the addition of micromolar amount of calcium ions under biological conditions via circular dichroism (CD) spectroscopy.

Investigations of protein conformational changes as a signal for apoptosis

255th National Meeting (2018)

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