Exploring Protein Structure, Function, and Aggregation Through Fluorine NMR

"Exploring protein structure, function, and aggregation through fluorine NMR"

Guest Speaker: Dr. Laura Hawk, Grand Valley State University

Thursday, Oct. 7th, 2021 @ 11:30a - 12:20p

Science Building 110

Fluorination of biomolecules and subsequent ¹⁹F NMR experiments permit facile exploration of the molecule of interest’s conformation and interactions with other molecules. This talk will discuss two applications of ¹⁹F NMR to biomolecules. To carry out ¹⁹F NMR experiments on OXA-66, a protein expressed by Acenitobacter baumanii that allows it to hydrolyze β-lactam antibiotics, its seven tryptophans were biosynthetically labeled with fluorine. Kinetics experiments with the fluorinated OXA-66 demonstrated that enzymatic activity was retained after fluorination. The ¹⁹F NMR resonances were assigned with site-directed mutagenesis. No changes were observed in the spectra of the fluorinated protein upon addition of a substrate or an inhibitor. Second, the kinetics of aggregation of the functional amyloid kassinin will be compared with those of toxic amyloids found in diseases such as Alzheimer’s and Parkinson’s diseases.