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dc.contributor.authorChoi, Monica Sunok
dc.date.accessioned2014-03-03T23:26:17Z
dc.date.available2014-03-03T23:26:17Z
dc.date.issued2005-12
dc.identifier.otherchoi_monica_s_200512_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/choi_monica_s_200512_ms
dc.identifier.urihttp://hdl.handle.net/10724/22886
dc.description.abstractDNA is constantly bombarded by endogenous reagents threatening their viability and genomic stability. The resulting products cause DNA lesions causing serious implications on cell health and mutagenesis. Recent biochemical assays allow the detection of various types of lesions, notably high performance liquid chromatography (HPLC) and mass spectrometry. Structural and biochemical studies have provided insight into DNA damage recognition and repair mechanisms. Research indicates both photolyase and DNA glycosylase have multiple interactions with the DNA phosphodeoxyribose backbone and perform lesion repair by base- flipping out of the helix and insertion into the enzyme pocket. Photolyase crystal structure strongly supports the electron transfer take place over van der Waals distance between the flavin and the lesion. Concerted efforts have suggested Uracil- DNA glycosylase recognize uracil through a “Serine- Proline pinch” mechanism and repair occurs through flipping the nucleotide into the enzyme active site.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectDNA lesion
dc.subjectPhotolyase
dc.subjectDNA glycosylase
dc.subjectDNA Repair
dc.subjectX-ray crystallography
dc.subjectUltraviolet radiation
dc.subjectMutagenesis
dc.titleDNA lesion recognition and repair mechanism by photolyase and DNA glycosylase
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorHenry F. Schaefer, III
dc.description.committeeHenry F. Schaefer, III
dc.description.committeePaul von Rague' Schleyer
dc.description.committeeRichard A. Dluhy


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