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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 ...
Experimental Kinetic Study to Explore the Impact of Macromolecular Crowding on Structure and Function of Escherichia coli Prolyl–tRNA Synthetase
Aminoacyl-tRNA synthetases (AARSs) are enzymes that catalyze the covalent attachment of amino acids to their cognate tRNA. This reaction is known as aminoacylation of tRNA and is crucial for protein synthesis in all living ...
Synthesis, Spectral Characterization, and Nucleic Acids Interactions of Nickel (II)-Salen complex
Around the world, cancer is one of the leading causes of death. DNA is the primary target molecule for most anticancer therapy. Transition metal complexes are known to have DNA binding and cleavage properties under ...
Exploring the Interplay of Dynamics and Catalysis in Escherichia coli Prolyl-tRNA Synthetase using Quantum Mechanical/Molecular Mechanical Simulations
The intrinsic dynamics that are inherent in proteins are known to be critical for many important biochemical processes. However, there is still limited information regarding how dynamics favor enzymes to achieve their ...