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dc.contributor.authorHamerly, Tim
dc.date.accessioned2012-05-15T14:05:22Z
dc.date.available2012-05-15T14:05:22Z
dc.date.created2010-11
dc.date.issued2012-05-15
dc.identifier.urihttp://hdl.handle.net/123456789/286
dc.description.abstractChiral recognition plays an important role in the many places including chiral chromatography and the biological world where many enzymes are enantioselective. Understanding how molecular micelles and enzymes like phosphotriesterase are able to detect and distinguish isomers can help explain how chiral drugs or compounds are consumed within the body. The binding of 1,1'-binaphthyl-2,2'-diyl hydrogen phosphate to a molecular micelle containing a dipeptide head group was explored using NMR spectroscopy. Similarly, enzyme kinetics were used to study how site-target mutagenesis affected the enzymatic site of phosphotriesterase. In both cases, it was found that a macromolecules ability to detect chirality changed when the residues within the binding pocket of each changed.en_US
dc.subjectChiral Recognitionen_US
dc.subjectPhosphotriesterase
dc.subjectMolecular Micelles
dc.subjectMolecular Micelles
dc.titleExamining the Mechanics of Chiral Recognition in Phosphotriesterase and Molecular Micellesen_US
dc.typeThesisen_US


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