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dc.contributor.authorHati, Sanchita
dc.contributor.authorLosbanos, Louis
dc.contributor.authorWeinzetl, Murphi
dc.contributor.authorAdams, Lauren
dc.contributor.authorHu, Huakun
dc.contributor.authorBhattacharyay, Sudeep
dc.date.accessioned2017-11-30T17:44:59Z
dc.date.available2017-11-30T17:44:59Z
dc.date.issued2017-11-30T17:44:59Z
dc.identifier.urihttp://digital.library.wisc.edu/1793/77420
dc.descriptionColor poster with text, models, charts, and tables.en
dc.description.abstractIn the present study, we have employed site-directed mutagenesis to probe the role of four residues in E. coli ProRS (Ec ProRS) on the overall catalytic function. Specifically, we examined the impact of changes in amino acid properties on the interactions between the enzyme (Ec ProRS) and the substrates, proline and ATP.en
dc.description.sponsorshipNational Institute of Health; University of Wisconsin--Eau Claire Office of Research and Sponsored Programs.en
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589;
dc.subjectEscherichia colien
dc.subjectChemistryen
dc.subjectProlyl-tRNA synthetaseen
dc.subjectPostersen
dc.titleInvestigating Catalytically Important Residues in Escherichia coli Prolyl-tRNA Synthetase Through Site-Directed Mutagenesisen
dc.typePresentationen


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