Gamma crystallin proteins can be found in the eye lens, helping to maintain transparency through their intermolecular interactions. Because crystallins remain in the lens after their initial synthesis, mutations caused by prolonged exposure to environmental stresses can have permanent consequences, including aggregation and liquid‐liquid phase separation of the crystallins. These structural deviations can cause clouding of the lens, a condition known as cataracts. With the use of light scattering and nuclear magnetic resonance (NMR) spectroscopy, we aim to study the detailed interactions between crystallins. We have expressed and isolated recombinant bovine Gamma B crystallin protein in Escherichia coli and performed T1/T2 NMR experiments to measure the longitudinal and transverse relaxation times of the protein. These experiments allowed us to analyze the crystallins in terms of the attractive forces between molecules and how those forces change with the manipulation of environmental conditions (temperature, pH). Analysis of our current data suggests higher rates of intermolecular interaction at higher concentrations of crystallins and lower temperatures.Support or Funding InformationRIT and NIH Grant EY018249This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.