Apoferritin Crystallization in relation to Eye Cataract.
Degree: PhD, Bioengineering, 2006, Georgia Tech
Protein crystallization is significant in both biotechnology and biomedical applications. In biotechnology, crystallization is essential for determining the structure of both native and synthesized therapeutically important proteins. It can also be used as a final purification step and as a stable form for protein storage. With regard to biomedical systems, protein crystallization appears to be involved in the development and manifestation of certain human diseases. In particular, there exists evidence that L-rich ferritin crystals are involved in Hereditary Hyperferritinemia Cataract Syndrome (HHCS).
In the current research a microbatch crystallization apparatus has been introduced that enables (1) multiple batch crystallization experiments at various temperatures and solution conditions in parallel and (2) quantitative monitoring of crystal growth without disturbing the progress of an experiment for observation. The primary application of the apparatus is, but not limited to, screening of protein crystallization conditions, although the system can also be used for other macromolecular and small-molecule crystallization experiments.
Multiwell microbatch experiments demonstrated the dependence of apoferritin crystal growth kinetics and final crystal size on temperature and cadmium concentration. Although the solubility of apoferritin might be independent of temperature, the results of this study show that the crystal growth kinetics are affected by temperature, profoundly under some conditions.
For apoferritin under near physiological conditions the solution thermodynamics in the form of the second virial coefficient have proofed to be a valuable predictor for the crystallization outcome. Furthermore, the significance of the elevated level of some divalent cations in cataractous lenses has been studied both in dilute solutions and under crystallization conditions and cadmium seems to be sole menace in apoferritin condensation.
Advisors/Committee Members: Ronald W. Rousseau (Committee Chair), Athanassios Sambanis (Committee Co-Chair), Joe LeDoux (Committee Member), Timothy M. Wick (Committee Member), Victor Breedveld (Committee Member).
Subjects/Keywords: Activation energy for crystallization; Cataract; Apoferritin; Second virial coefficient; Crystallization; Thermal gradient; Light Scattering; Microbatch
to Zotero / EndNote / Reference
APA (6th Edition):
Bartling, K. (2006). Apoferritin Crystallization in relation to Eye Cataract. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/14111
Chicago Manual of Style (16th Edition):
Bartling, Karsten. “Apoferritin Crystallization in relation to Eye Cataract.” 2006. Doctoral Dissertation, Georgia Tech. Accessed January 27, 2021.
MLA Handbook (7th Edition):
Bartling, Karsten. “Apoferritin Crystallization in relation to Eye Cataract.” 2006. Web. 27 Jan 2021.
Bartling K. Apoferritin Crystallization in relation to Eye Cataract. [Internet] [Doctoral dissertation]. Georgia Tech; 2006. [cited 2021 Jan 27].
Available from: http://hdl.handle.net/1853/14111.
Council of Science Editors:
Bartling K. Apoferritin Crystallization in relation to Eye Cataract. [Doctoral Dissertation]. Georgia Tech; 2006. Available from: http://hdl.handle.net/1853/14111