Experimental determination of probable charges on individual residues in gamma B crystallin by nuclear magnetic resonance spectroscopy
Olivia Fraser, RIT Chemistry M.S. Candidate
Co-Advisors: Dr. Lea Michel and Dr. George Thurston
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Gamma B crystallin is the bovine homolog to the human lens gamma D crystallin protein. Abnormalities, such as single point mutations, in crystallin proteins have been implicated in cataracts, a condition where loss of protein solubility in the eye lens leads to partial or total blindness due to lens cloudiness. In addition, changes in interactions between crystallin proteins due to altered electrostatic effects can contribute to phase separation in the lens. In order to better understand these protein-protein interactions, it is necessary to first describe the probable charge patterns on the proteins. These charge patterns greatly impact inter-protein interactions and therefore have an effect on liquid-liquid phase separation in the lens. Dr. Thurston’s lab group has previously developed a model to map charge patterns on gamma crystallin and predict those charge probabilities at low protein concentrations. Here, we describe our efforts to measure the acidity of individual gamma B crystallin residues using nuclear magnetic resonance spectroscopy and other computational methods.
Olivia Fraser graduated with a B.S. degree in Chemistry from St. John Fisher College in 2018. As an undergraduate, she conducted physical chemistry research through programs at RIT, St. John Fisher College, and Penn State. Outside of chemistry, Olivia enjoys volunteer work and is involved with coaching for Science Olympiad, a program that engages students in STEM fields from a young age.
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