Show full item record

File(s):

Author(s)

Mueller, Irene C.; Cao, Bach; Meitzner, Karl J.; Tschudy, Matthew J.

Advisor(s)

Bhattacharyya, Sudeep; Hati, Sanchita

Date

May 2011

Subject(s)

Catalytic RNA; Functional analysis; Escherichia coli; Lysine; Posters; Ligases; Microbiological synthesis

Series

USGZE AS589

Abstract

The Escherichia coli (Ec) prolyl-tRNA synthetase enzyme possesses three distinct domains. One of the domains, the editing domain, is critical for proofreading the charged tRNAPro, ensuring the correct amino acid has been attached to the tRNA molecule. In this editing domain, a highly conserved lysine has been found to be absolutely essential for proofreading. Through site-directed mutagenesis and enzyme kinetic studies this study attempted to probe the role of this lysine residue (K279).

Description

Color poster with text, diagrams, charts, and graphs.

Sponsor(s)

University of Wisconsin--Eau Claire Office of Research and Sponsored Programs; NIH-AREA grant

Permanent link

http://digital.library.wisc.edu/1793/55083 

Export

Export to RefWorks 

​

Part of

Student Research Day

Show full item record