2026-09-21T04:31:27Zhttps://wakespace.lib.wfu.edu/server/oai/request

oai:null:10339/474522026-09-02T11:06:30Zcom_10339_14934col_10339_38132

Sharma, Sandhya Bharti 2015-01-21T09:35:16Z 2017-01-21T09:30:13Z 2014 https://wakespace.lib.wfu.edu/handle/10339/47452 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. en Wake Forest University Aminotransferase MetRS AARSs MpMetRS protein purification enzyme kinetic analysis BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES Dissertation Alexander, Rebecca W. Dos Santos, Patricia C. Comstock-Ferguson, Lindsay R. Muday, Gloria K. Welker, Mark E. Chemistry 2017-01-21 open.access