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dc.contributor.advisorDeardorff, Don
dc.contributor.authorPace, Andrew
dc.contributor.authorCanon, Jeffrey
dc.contributor.authorWatts, Kathryn
dc.date.accessioned2020-08-13T14:55:51Z
dc.date.available2020-08-13T14:55:51Z
dc.date.issued2004-01-01 0:00
dc.identifier.urihttps://scholar.oxy.edu/handle/20.500.12711/552
dc.description.abstractEnantiomerically pure substances are extremely important in producing pharmaceuticals and other biologically important chemicals. To produce enantiomerically pure compounds is difficult because they have identical physical properties; this makes the separation of enantiomers nearly impossible. Our research, however, uses the enzyme Oxinitrilase to create an enantiomerically pure base molecule that can be easily manipulated into more useful compounds. As such, no difficult separations are necessary. We then couple this enzymatic chemistry with two synthetic catalysts?a ruthenium Grubbs and a palladium (0) catalyst. This methodology provides access to several synthetically and biologically important molecules, including Anisomycin, Prozac, and a family of glycosidase inhibitors.
dc.description.sponsorshipSupport provided by:The Arnold and Mabel Beckman Scholars Award, NSF-Research Experience for Undergraduates in Chemistry Grant Fellowship, Sherman Fairchild Foundation Grant Fellowship, and the Howard Hughes Medical Institute Grant Fellowship
dc.titleElaboration of an Enzymatically-Derived Fragment via Olefin Cross-Metathesis. Andrew Pace, Jeffrey Cannon, Jason Papazian and Kathryn Watts
dc.typearticle
dc.abstract.formathtml
dc.description.departmentchem
dc.source.issueurc_student
dc.source.issueurc_student
dc.identifier.legacyhttps://scholar.oxy.edu/urc_student/287
dc.source.statuspublished


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