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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 ...
Experimental Kinetic Study to Explore the Impact of Macromolecular Crowding on Structure and Function of Escherichia coli Prolyl–tRNA Synthetase
(2017-03-17)
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 ...
Exploring the Interplay of Dynamics and Catalysis in Escherichia coli Prolyl-tRNA Synthetase using Quantum Mechanical/Molecular Mechanical Simulations
(2017-03-20)
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 ...
Spectroscopic Studies to Explore the Impact of Macromolecular Crowding on the Structure and Function of Escherichia coli of Prolyl-tRNA Synthetase
(2016-10-14)
Most computational and experimental studies to understand the molecular mechanism of an enzyme-catalyzed reaction are usually performed in dilute solutions. However, enzymatic activities in vivo occur in a crowded environment ...
How Does Varying Sizes and Concentrations of Poly(Ethylene Glycol) Affect the Conformation and Function of the Enzyme Escherichia Coli Prolyl-Trna Synthetase?
(2021-04)
Poly(ethylene glycol) (PEG) is a biocompatible, hydrophilic, flexible, non-toxic polyether commonly used in proteomics because it is widely regarded to be a biologically inert molecule. This includes PEG2000 (molecular ...