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dc.contributor.authorSaladino, Jessica Marie
dc.date.accessioned2014-03-04T20:22:29Z
dc.date.available2014-03-04T20:22:29Z
dc.date.issued2011-08
dc.identifier.othersaladino_jessica_m_201108_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/saladino_jessica_m_201108_ms
dc.identifier.urihttp://hdl.handle.net/10724/27583
dc.description.abstractReactive oxygen species (ROS) are known to cause significant damage in physiological processes and have been implicated in many diseases and pathological conditions. However, the complex mixture of products that result from protein-ROS chemistry has made it difficult to study the effects of oxidative damage on proteins. A better understanding of the way ROS, including hydroxyl radicals, affect proteins and the conformational changes they induce are crucial to understanding the conditions associated with oxidative stress. In order to understand this mechanism at a molecular level, it is necessary to be able to ascertain the sites of oxidation and level of oxidation at different sites in damaged proteins. Protein-hydroxyl radical chemistry is also exploited as a biophysical tool to study protein structure, protein folding, protein-protein interactions, and protein-ligand interactions. This work seeks to improve current techniques for identification and quantitation of sites of oxidation and oxidation products at different sites.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectMass spectrometry
dc.subjectQTOF
dc.subjectImmonium ion
dc.subjectElectron capture dissociation
dc.subjectHydroxyl-radical
dc.subjectFootprinting
dc.titleIdentifying and quantifying hydroxyl radical oxidation products in peptides and proteins using improved mass spectrometric techniques
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorJoshua Sharp
dc.description.committeeJoshua Sharp
dc.description.committeeRon Orlando
dc.description.committeeI. Jonathan Amster


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