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BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES

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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.
subject
Aminotransferase
MetRS
AARSs
MpMetRS
protein purification
enzyme kinetic analysis
contributor
Sharma, Sandhya Bharti (author)
Alexander, Rebecca W. (committee chair)
Dos Santos, Patricia C. (committee member)
Comstock-Ferguson, Lindsay R. (committee member)
Muday, Gloria K. (committee member)
Welker, Mark E. (committee member)
date
2015-01-21T09:35:16Z (accessioned)
2017-01-21T09:30:13Z (available)
2014 (issued)
degree
Chemistry (discipline)
embargo
2017-01-21 (terms)
identifier
http://hdl.handle.net/10339/47452 (uri)
language
en (iso)
publisher
Wake Forest University
title
BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES
type
Dissertation

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