Small Angle X-Ray Scattering and Form Factor Modeling of β Crystallins - a Physiologically Significant Eye Lens Cytoplasm Protein

This thesis provides in depth analysis of small angle x-ray scattering (SAXS) experiments conducted on the beta-high crystallin eye lens cytoplasm protein. In particular, radius of gyration and molecular weight measurements are extracted and compared to measurements from existing work. Furthermore, an approach to math ematically modeling the scattering ”form-factor”, which describes the size and shape of individual particles, is also developed and applied to the SAXS data. The model acheived in the thesis appears to agree closely with scattering data at the low q range. Several obstacles which impede the resulting modeling from perfectly characterizing the data at higher q ranges, such as the presence of intrinsically disordered regions and oligomeric complexity are discussed. Potential methods and techniques to im prove on the model outlined in the thesis in the future, such as molecular dynamics simulations, consideration of protein docking servers like ClusPro, and SAXS fitting algorthims like SASREF, are also discussed.