Title:
Apoferritin Crystallization in relation to Eye Cataract

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dc.contributor.advisor Rousseau, Ronald W.
dc.contributor.advisor Sambanis, Athanassios
dc.contributor.author Bartling, Karsten en_US
dc.contributor.committeeMember LeDoux, Joseph M.
dc.contributor.committeeMember Timothy M. Wick
dc.contributor.committeeMember Victor Breedveld
dc.contributor.department Bioengineering en_US
dc.date.accessioned 2007-03-27T18:24:28Z
dc.date.available 2007-03-27T18:24:28Z
dc.date.issued 2006-08-22 en_US
dc.description.abstract 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. en_US
dc.description.degree Ph.D. en_US
dc.format.extent 3179961 bytes
dc.format.mimetype application/pdf
dc.identifier.uri http://hdl.handle.net/1853/14111
dc.language.iso en_US
dc.publisher Georgia Institute of Technology en_US
dc.subject Activation energy for crystallization en_US
dc.subject Cataract en_US
dc.subject Apoferritin en_US
dc.subject Second virial coefficient en_US
dc.subject Crystallization en_US
dc.subject Thermal gradient en_US
dc.subject Light Scattering en_US
dc.subject Microbatch en_US
dc.title Apoferritin Crystallization in relation to Eye Cataract en_US
dc.type Text
dc.type.genre Dissertation
dspace.entity.type Publication
local.contributor.advisor Rousseau, Ronald W.
local.contributor.advisor Sambanis, Athanassios
local.contributor.corporatename College of Engineering
local.contributor.corporatename College of Engineering
local.relation.ispartofseries Doctor of Philosophy with a Major in Bioengineering
relation.isAdvisorOfPublication 54a1d094-6cef-41c7-8168-e36b41eaf4f7
relation.isAdvisorOfPublication 90a12241-15c3-4cbf-bc27-724c028b8fc1
relation.isOrgUnitOfPublication 7c022d60-21d5-497c-b552-95e489a06569
relation.isOrgUnitOfPublication 7c022d60-21d5-497c-b552-95e489a06569
relation.isSeriesOfPublication 5db25cda-aa52-48d2-8f63-c551ef2c92f4
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