Research in the Hebda Lab centers around understanding protein-protein interactions. We study this interactions by using the protein Alpha Crystallin, which is about 40% of the protein in your eye lens and helps resist the formation of cataracts. Understanding and perhaps extending the function of this protein could reduce the occurrence of cataracts. This protein self-associates with many copies of itself into large oligomers and functions as a chaperone. A chaperone is a protein that recognizes and interacts with damaged or unfolded proteins to prevent their aggregation. It is damaged, aggregated proteins that cause the light scattering deposits we call cataracts. This protein system therefor allows us to study functional self-association that gives rise to function recognition of damaged proteins.
In the lab students would work to produce human and mutant versions of this protein in E. coli, purify the protein using protein chromatography, and study their function using several spectroscopic techniques such as light scatter, absorption, and fluorescence. By mutating the protein to specifically change key residues the lab seeks to better understand the molecular causes that govern oligomerization and chaperone function.