Protein aggregation is a phenomenon that plays a major role in protein crystallization and in protein formulation. In protein crystallization, aggregation is the prerequisite step; however, in protein formulation it has to be suppressed to assure therapeutic efficiency of the product. Light scattering techniques are the most promising methods to study the hydrodynamic properties of macromolecular solutions, which directly measures protein aggregation. Unfortunately, the normal dynamic light scattering technique is regarded as expensive because of the amount of protein used for these experiments. In order to address this problem, a scale down dynamic light scattering device has been designed. The osmotic second virial coefficient, a dilute solution parameter helps in identifying solution conditions for protein crystal growth. The second part of this thesis involves comparison of osmotic second virial coefficient (B) measurements of lysozyme using laser light scattering techniques with B measurements of lysozyme performed using self-interaction chromatography (SIC).
| Identifer | oai:union.ndltd.org:MSSTATE/oai:scholarsjunction.msstate.edu:td-2276 |
| Date | 15 December 2007 |
| Creators | Parupudi, Arun Kumar |
| Publisher | Scholars Junction |
| Source Sets | Mississippi State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
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