Title:
Application of Spectroscopy to Protein Characterization

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dc.contributor.advisor El-Sayed, Mostafa A.
dc.contributor.author Sanii, Laurie Shireen en_US
dc.contributor.committeeMember Liotta, Charles L.
dc.contributor.committeeMember John Zhang
dc.contributor.committeeMember Laren Tolbert
dc.contributor.committeeMember Mohan Srinivasarao
dc.contributor.department Chemistry and Biochemistry en_US
dc.date.accessioned 2006-01-19T21:07:51Z
dc.date.available 2006-01-19T21:07:51Z
dc.date.issued 2005-11-11 en_US
dc.description.abstract There are two contributions of this thesis. The first contribution, described in chapters one through six, involves studing the relationship between the protein packing structure of bacteriorhodopsin (bR) and its function as a proton pump. In 2002, a novel crystallization method published by Bowie and Farham resulted in an unusual antiparallel monomeric packing structure of bicelle bacteriorhodopsin (bcbR) crystals, the spectroscopic properties of which had not been studied. In this thesis, these bicelle bR crystals are investigated to better understand how the changes in the protein tertiary structure affect the function. Specifically: Does the retinal Schiff base retain its ability to isomerize in this unusual protein packing structure of bR? How is the hydration of its binding pocket affected? Does the protein retain the ability to undergo the photocycle and pump protons? If so, how are the rates of the deprotonation/reprotonation of the Schiff base affected by the antiparallel monomer packing structure of the protein? Is Asp85 still the proton acceptor during the deprotonation process of the photocycle? The second contribution of the thesis, described in chapter seven, describes the surface attachment and growth of the biofilm formed by the pathogenic bacterium Streptococcus pneumoniae using attenuated total reflection/Fourier transform infrared spectroscopy (ATR/FTIR). This organism was chosen for its clinical significance; it is one of the organisms suspected in forming biofilms in individuals who develop otitis media, one of the most common causes of ear infections of childhood. In contrast to previous ATR/FTIR experiments examining the formation of biofilms on surfaces, this method is unique in that it combines two techniques - ATR/FTIR and Epifluorescence microscopy which when used together allow for the simultaneous monitoring of the IR spectrum of the S. pneumoniae biofilm as it develops and as provides a method for quantifying total and viable cell counts at various stages during the development. en_US
dc.description.degree Ph.D. en_US
dc.format.extent 5005364 bytes
dc.format.mimetype application/pdf
dc.identifier.uri http://hdl.handle.net/1853/7641
dc.language.iso en_US
dc.publisher Georgia Institute of Technology en_US
dc.subject Bacteriorhodopsin en_US
dc.subject Bicelle
dc.subject Crystals
dc.subject Raman
dc.subject FTIR
dc.subject.lcsh Raman spectroscopy en_US
dc.subject.lcsh Spectrum analysis en_US
dc.subject.lcsh Bacteriorhodopsin en_US
dc.subject.lcsh Crystals en_US
dc.subject.lcsh Fourier transform infrared spectroscopy en_US
dc.subject.lcsh Proteins Analysis en_US
dc.title Application of Spectroscopy to Protein Characterization en_US
dc.type Text
dc.type.genre Dissertation
dspace.entity.type Publication
local.contributor.advisor El-Sayed, Mostafa A.
local.contributor.corporatename School of Chemistry and Biochemistry
local.contributor.corporatename College of Sciences
relation.isAdvisorOfPublication 2f075506-30f5-42e0-b0a8-9da9ecd0b6bd
relation.isOrgUnitOfPublication f1725b93-3ab8-4c47-a4c3-3596c03d6f1e
relation.isOrgUnitOfPublication 85042be6-2d68-4e07-b384-e1f908fae48a
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