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Investigating Catalytically Important Residues in Escherichia coli Prolyl-tRNA Synthetase Through Site-Directed Mutagenesis
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 ...
Investigating Catalytically Important in Escherichia coli Prolyl-tRNA Synthetase Using SiteDirected Mutagenesis and Computational Studies
This research project is a continuing effort focused on the molecular-level understanding of the relationship between structure, dynamics, and function in aminoacyl-tRNA synthetases (AARSs). Recent computational studies ...
Investigating Structure-Dynamics-Function Differences Among Various Species of Proyl-tRNA Synthetase Using a Hybrid QM/MM Computational Technique
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, ...
Site-Directed Mutagenesis and Intrinsic Tryptophan Fluorescence Study to Probe the Conformational Change in Escherichia coli Prolyl-tRNA Synthetase (Ec ProRS)
Amino-acyl tRNA synthetases (AARSs) belong to a class of an important family of enzymes that are critical for proteins biosynthesis in all living organisms. They catalyze aminoacylation of tRNAs, a key step in protein ...