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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 ...
Exploring the Role of Distant Domain Dynamics in Substrate Binding of Escherichia Coli Prolyl-tRNA Synthetase
Our results demonstrate that the presence of the INS is critical to provide the required energy barrier for the substrate to be bound to the catalytic core, instead of getting spontaneously hydrolyzed.
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, ...