Abstract

γB – crystallin is a 21 kDa protein found in the lens of the bovine eye, existing without turnover. It shares 76% sequence identity with a human lens protein, γD – crystallin, with a structural RMSD of 0.8 Å by Dali (174 residues, Cα atoms only). Damages to and abnormalities on crystallin proteins can lead to phase separation and aggregation in the lens, resulting from aberrant inter-protein interactions, which can lead to partial or total blindness by cataract. The purpose of this work is to elucidate global inter-protein interactions of wild-type γB – crystallin by T1 and T2 relaxation NMR spectroscopy experiments with increasing temperatures and protein concentrations. We determined that rotational diffusion is significantly slowed with increasing concentration, even when taking into consideration the viscosity changes. The primary focus of this work has been the investigation of the exponential fit of the T1 decay, and specifically identifying potential explanations for the unusual double-exponential fit for these data.

Publication Date

5-2020

Document Type

Thesis

Student Type

Graduate

Degree Name

Chemistry (MS)

Department, Program, or Center

School of Chemistry and Materials Science (COS)

Advisor

Lea Michel

Advisor/Committee Member

George Thurston

Advisor/Committee Member

Jeffrey Mils

Campus

RIT – Main Campus

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