Abstract
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
Publication Date
12-2022
Document Type
Thesis
Student Type
Graduate
Degree Name
Physics (MS)
Department, Program, or Center
School of Physics and Astronomy (COS)
Advisor
Michael Kotlarchyk
Advisor/Committee Member
David Ross
Advisor/Committee Member
Lishibanya Mohapatra
Recommended Citation
LaRose, Malcolm F., "Light Scattering Study of an Important Eye Lens Protein: Beta Crystallin" (2022). Thesis. Rochester Institute of Technology. Accessed from
https://repository.rit.edu/theses/11386
Campus
RIT – Main Campus
Plan Codes
PHYS-MS