Document Type


Publication Date



Chemistry | Organic Chemistry


Henry Jakubowski


Recently, biomedical science has turned its drug research endeavors towards a philosophy known as rational drug design. Its goal is to avoid the guesswork and instead design and create the exact proteins that are needed. In order for rational drug design to be feasible, a better understanding of protein structure and function needs to be obtained. This research analyses the structure and function of a "rationally" designed mutation of the calcium binding protein parvalbumin. Parvalbumin was chosen because certain aspects of its composition facilitate analysis and in addition, there is extensive data already known about the protein. The mutation involved the alteration of three amino acids in its sequence to create a zinc binding site. Zinc plays an important role in stabilizing the tertiary structure of many enzymes that bind DNA. The ability to create a zinc binding site on biological proteins would open up numerous opportunities in the process of drug design.

The ultimate goal of the project was to determine if the protein showed a significant affinity for zinc at the designed binding site. This was attempted by performing a series of spectroscopic and optical analyses on both the mutant and a wild-type parvalbumin obtained from cod. These studies include emission, anisotropy, rotational polarization, lifetime, and circular dichromism measurements.