Item Details

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