(491.6) Elucidating the Effect of Point Mutations on Gamma B Crystallin Protein Interactions
Sunday, April 3, 2022
12:45 PM – 2:00 PM
Location: Exhibit/Poster Hall A-B - Pennsylvania Convention Center
Poster Board Number: A114
Natalie Labbe (Rochester Institute of Technology), Lea Michel (Rochester Institute of Technology), George Thurston (Rochester Institute of Technology), Jeffrey Mills (Rochester Institute of Technology), Zach Williams (Rochester Institute of Technology), Jimmy Hasselbeck (Rochester Institute of Technology), Lucas Cirrincione (Rochester Institute of Technology)
Presenting Author Rochester Institute of Technology
Cataracts form when crystallin proteins in the eye lens undergo phase separation or aggregation, thereby failing to maintain lens transparency. Mutations in the amino acid sequence of the crystallins can alter the structure and/or chemical properties of the proteins, resulting in increased inter-protein interactions, increased aggregation, or changes to the proteins’ phase diagram, all of which can enhance cataract formation. Here, we describe our work on γB crystallin, the bovine homologue to human γD crystallin, and two site-directed mutants of γB crystallin with known links to congenital cataracts. Using nuclear magnetic resonance spectroscopy, we aim to determine how inter-protein interactions of bovine γB crystallin are altered by point mutations so that we can gain a better understanding of the mechanism behind cataract formation. Results from preliminary experiments suggest that the inter-protein interactions of γB crystallin are highly dependent on environmental conditions, such as temperature, pH, and protein concentration, and studies are underway to compare those behaviors to the behavior of mutant proteins under similar conditions.
