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dc.contributor.authorStoudemayer, Melissa Joyce
dc.date.accessioned2015-04-29T04:30:11Z
dc.date.available2015-04-29T04:30:11Z
dc.date.issued2014-08
dc.identifier.otherstoudemayer_melissa_j_201408_phd
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/stoudemayer_melissa_j_201408_phd
dc.identifier.urihttp://hdl.handle.net/10724/31314
dc.description.abstractFourier transform ion cyclotron mass spectrometry (FT-ICR) is a very powerful technique that is well suited for the analysis of many types of biomolecules. This dissertation presents four experiments utilizing the strengths of FT-ICR. The first experiment presented evaluates the use of accurate mass measurement and nitrogen stoichiometry to characterize the proteome of Acinetobacter baylyi ADP1. Then, accurate mass measurements, paired with endogenous labeling, are used to investigate the metabolic pathway of dimethylsulphoniopropionate in Ruegeria pomeroyi DSS-3. The next analysis investigates the robustness and effectiveness of using chemical crosslinking and mass defect labeling as a means of detecting and evaluating reaction products in individual proteins and peptides. The last topic presented examines the various factors responsible for the generation of an uncommon ion, [M-H]+ in a set of synthesized curcumin analogues.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectFourier transform ion cyclotron mass spectrometry (FT-ICR)
dc.subjectMass spectrometry, Electrospray ionization (ESI)
dc.subjectMatrix assisted laser desorption ionization (MALDI)
dc.subjectShotgun proteomics
dc.subjectAccurate mass measurement
dc.subjectNitrogen stoichiometry
dc.subjectMass defect labeling
dc.subjectChemical crosslinking
dc.subjectCurcumin analogues
dc.titleFourier transform ion cyclotron resonance mass spectrometry methodologies for the analysis of biomolecules
dc.typeDissertation
dc.description.degreePhD
dc.description.departmentChemistry
dc.description.majorChemistry


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