Light scattering experiments were performed on bovine βH crystallin, an important protein component of the mammalian eye lens. Light scattering results are compared to simplified models for the free energy of mixing of β crystallins with water. The static light scattering data are well-represented by hard convex body equations of state having dimensionless non-sphericity coefficients of close to 2, compatible with prolate spherocylinders, and weight-average molecular weights ranging between 2−5×105 g/mole. Additionally, quasi-elastic light scattering data was obtained which shows that βH has a hydrodynamic radius near 7.3 nm. These experiments extend light scattering work on β crystallins well into the realm of concentrations in which short-range order between proteins dramatically reduces light scattering efficiency, as occurs in the eye lens cytoplasm.
Library of Congress Subject Headings
Eye--Molecular aspects; Crystalline lens; Proteins--Analysis; Light--Scattering
Department, Program, or Center
School of Physics and Astronomy (COS)
LaRose, Malcolm F., "Light Scattering Study of an Important Eye Lens Protein: Beta Crystallin" (2022). Thesis. Rochester Institute of Technology. Accessed from
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