{"id":{"repo_id":"wfu","oai_identifier":"oai:wakespace.lib.wfu.edu:10339/47452"},"canonical_url":"https://search.dev.ndltd.org/etd/wfu/oai:wakespace.lib.wfu.edu:10339/47452","repository":{"repo_id":"wfu","name":"Wake Forest University","base_url":"https://wakespace.lib.wfu.edu/oai/request"},"display":{"title":"BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES","abstract":"Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different organisms. MetRS is proposed to use long-range communication between its anticodon binding and catalytic active sites. MetRS also exhibits structural variability in different organisms including different oligomeric states and appended domains. In this dissertation, our goal was to understand how long-range communication occurs in E. coli MetRS and what additional functions are contributed by the large appended domain of M. penetrans MetRS.","abstract_html":"Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different organisms. MetRS is proposed to use long-range communication between its anticodon binding and catalytic active sites. MetRS also exhibits structural variability in different organisms including different oligomeric states and appended domains. In this dissertation, our goal was to understand how long-range communication occurs in E. coli MetRS and what additional functions are contributed by the large appended domain of M. penetrans MetRS.","abstract_has_math":false,"creators":["Sharma, Sandhya Bharti"],"institution":"Wake Forest University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014","date_published":"2014","updated_at":"2026-07-27T22:01:46Z","subjects":["Aminotransferase"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10339/47452","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Sharma, Sandhya Bharti"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2015-01-21T09:35:16Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2017-01-21T09:30:13Z"]},{"key":"dc:date.issued","label":"Date","values":["2014"]},{"key":"dc:publisher","label":"Institution","values":["Wake Forest University"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Aminotransferase"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10339/47452"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different organisms. MetRS is proposed to use long-range communication between its anticodon binding and catalytic active sites. MetRS also exhibits structural variability in different organisms including different oligomeric states and appended domains. In this dissertation, our goal was to understand how long-range communication occurs in E. coli MetRS and what additional functions are contributed by the large appended domain of M. penetrans MetRS."]},{"key":"dc:title","label":"Title","values":["BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES"]}]}],"canonical_facts":{"dc:creator":["Sharma, Sandhya Bharti"],"dc:date.accessioned":["2015-01-21T09:35:16Z"],"dc:date.available":["2017-01-21T09:30:13Z"],"dc:date.issued":["2014"],"dc:description.abstract":["Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different organisms. MetRS is proposed to use long-range communication between its anticodon binding and catalytic active sites. MetRS also exhibits structural variability in different organisms including different oligomeric states and appended domains. In this dissertation, our goal was to understand how long-range communication occurs in E. coli MetRS and what additional functions are contributed by the large appended domain of M. penetrans MetRS."],"dc:identifier.uri":["http://hdl.handle.net/10339/47452"],"dc:language.iso":["en"],"dc:publisher":["Wake Forest University"],"dc:subject":["Aminotransferase"],"dc:title":["BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES"],"dc:type":["Dissertation"]},"updated_at":"2026-07-27T22:01:46Z"}