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Investigating Catalytically Important Residues in Escherichia coli Prolyl-tRNA Synthetase Through Site-Directed Mutagenesis
(2017-11-30)
In the present study, we have employed
site-directed mutagenesis to probe the role of four residues in E. coli ProRS (Ec
ProRS) on the overall catalytic function. Specifically, we examined the impact of
changes in amino ...
Calculation of Binding Free Energies of NAD(P)H:Quinone Oxidoreductase 1 Inhibitors
(2018-04)
NAD(P)H:quinone oxidoreductase 1 (NQO1) plays a key role in cellular defense in humans. It is known to reduce quinones to hydroquinones, inhibiting their ability to become a free radical semiquinone state, and cause cellular ...
Investigating Structure-Dynamics-Function Differences Among Various Species of Proyl-tRNA Synthetase Using a Hybrid QM/MM Computational Technique
(2019-05)
All living organisms contain amino-acyl tRNA synthetases (AARSs) ‒ a family of enzymes critical for protein synthesis. They are responsible for the covalent ligation of proline to its specific tRNA molecule, called tRNAPro, ...
Use of Geometrical Docking Algorithm to Explore Species Specific Differences in Proyl-tRNA Synthetases
(2018-02-08)
Prolyl-tRNA synthetases belong to a class of enzymes that play a pivotal role in
the protein synthesis. These enzymes are responsible for attaching the amino
acid, proline, to the 3’ end of the prolyl-tRNA. The structures ...