Biochemical Studies to Probe the Domain-Domain Communication Pathways in E. coli Prolyl-tRNA Synthetase
| dc.contributor.advisor | Hati, Sanchita | |
| dc.contributor.author | Schmit, Heidi | |
| dc.date.accessioned | 2013-11-22T15:58:12Z | |
| dc.date.available | 2013-11-22T15:58:12Z | |
| dc.date.issued | 2013-05 | |
| dc.description | Color poster with texts, charts, images, and tables. | en |
| dc.description.abstract | Aminoacyl-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.sponsorship | National Institute of Health; National Science Foundation; University of Wisconsin--Eau Claire Office of Research and Sponsored Programs. | en |
| dc.identifier.uri | http://digital.library.wisc.edu/1793/67281 | |
| dc.language.iso | en_US | en |
| dc.relation.ispartofseries | USGZE AS589 | en |
| dc.subject | Escherichia coli | en |
| dc.subject | Catalytic RNA | en |
| dc.subject | Functional analysis | en |
| dc.subject | Interdomain communication | en |
| dc.subject | Mutagenesis | en |
| dc.subject | Posters | en |
| dc.title | Biochemical Studies to Probe the Domain-Domain Communication Pathways in E. coli Prolyl-tRNA Synthetase | en |
| dc.type | Presentation | en |
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