Protein denaturing plays important roles in the biological world. Understanding how proteins unfold allows scientists to understand structure alignment, bond forming/breaking, and even how the protein moves within a solution. Bovine serum albumin (BSA) is a plasma protein that has three domains. Acrylodan was covalently attached to BSA on Cysteine-34 which is located in the first domain. Sodium dodecyl sulfate (SDS) and trihexyl (tetradecyl) phosphonium chloride were used as different denaturants. SDS was added with quantifying increments up to 2 mM. The data showed that trihexyl (tetradecyl) phosphonium chloride had the same denaturing effect as SDS but with a 10 fold decrease in concentration in order to denature BSA. Both SDS and trihexyl (tetradecyl) phosphonium chloride showed an increasing blue shift. This presentation will focus on details of the denaturing process of BSA and how BSA is affected by the denaturant solutions.
|Presenter:||Michael Molnar (Undergraduate Student)|
|Time:||1:15 pm (Session III)
Please note that presentation times are approximate. If you are interested in attending sessions with multiple presentations, please be in the room at the start of the session.