Biochemical Studies to Probe the Domain-Domain Communication Pathways in E. coli Prolyl-tRNA Synthetase

dc.contributor.advisorHati, Sanchita
dc.contributor.authorSchmit, Heidi
dc.date.accessioned2013-11-22T15:58:12Z
dc.date.available2013-11-22T15:58:12Z
dc.date.issued2013-05
dc.descriptionColor poster with texts, charts, images, and tables.en
dc.description.abstractAminoacyl-tRNA synthetases (AARSs) are a family of enzymes that catalyze the covalent attachment of amino acids to their corresponding transfer-RNA. These enzymes play critical roles in protein synthesis and viability. AARSs are comprised of many domains and each domain is responsible for carrying out a specific function for the proper attachment of correct amino acids to tRNAs. This study specifically focused on one enzyme of this family--prolyl-tRNA synthetases (ProRS), which attaches proline on to the tRNA[superscript]Pro. The purpose of this study was to identify the role of specific mutations in the inter-domain communication and catalytic activity of this enzyme.en
dc.description.sponsorshipNational Institute of Health; National Science Foundation; University of Wisconsin--Eau Claire Office of Research and Sponsored Programs.en
dc.identifier.urihttp://digital.library.wisc.edu/1793/67281
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectEscherichia colien
dc.subjectCatalytic RNAen
dc.subjectFunctional analysisen
dc.subjectInterdomain communicationen
dc.subjectMutagenesisen
dc.subjectPostersen
dc.titleBiochemical Studies to Probe the Domain-Domain Communication Pathways in E. coli Prolyl-tRNA Synthetaseen
dc.typePresentationen

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