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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 ...
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 ...
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, ...
Studying the Interactions between Monosaccharide / Polysaccharide with Tryptophan Using Fluorescence Spectroscopy
Fluorescence spectroscopy has become a pivotal tool in biochemical research by virtue of its robustness and high sensitivity. Intrinsic protein fluorescence, that originates mainly from the aromatic amino acid tryptophan, ...
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 ...
Molecular Dynamics Simulation Studies to Probe the Impact of Oxidative Stress on the Binding of SARS-CoV-2 Spike Protein to Angiotensin-Converting Enzyme 2
The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein as well as the human cell surface receptor angiotensin-converting enzyme II (ACE2) contain several cysteine residues. These cysteine residues exist either in ...