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Site-Directed Mutagenesis and Intrinsic Tryptophan Fluorescence Study to Probe the Conformational Change in Escherichia coli Prolyl-tRNA Synthetase (Ec ProRS)
(2019-05)
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 ...
Studying the Interactions between Monosaccharide / Polysaccharide with Tryptophan Using Fluorescence Spectroscopy
(2019)
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, ...
Calculation of Binding Free Energies of NAD(P)H:Quinone Oxidoreductase 1 Inhibitors
(2018-04)
NAD(P)H:quinone oxidoreductase 1 (NQO1) plays a key role in cellular defense in humans. It is known to reduce quinones to hydroquinones, inhibiting their ability to become a free radical semiquinone state, and cause cellular ...
Investigating Catalytically Important in Escherichia coli Prolyl-tRNA Synthetase Using SiteDirected Mutagenesis and Computational Studies
(2018-05)
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 ...
Towards Development of a Computational Screening Tool for Quinone Oxidoreductase Inhibitors
(2019-05)
NAD(P)H:quinone oxidoreductase 1 (NQO1) and its paralog NRH:quinone
oxidoreductase 2 (NQO2) function by reducing quinones into hydroquinones via a two-electron reduction, which is mediated by the cofactor flavin adenine ...
Energetics of Hydride Transfer Reactions in Quinone Reductase 2
(2012-04)
Quinone Reductases belong to the class of flavin-dependent oxidoreductases. With its redox active cofactor flavin adenine dinucleotide (FAD), quinone reductases are known to utilize a ping pong kinetic mechanism during ...
Investigating Structure-Dynamics-Function Differences Among Various Species of Proyl-tRNA Synthetase Using a Hybrid QM/MM Computational Technique
(2019-05)
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, ...
Application of Statistical-Thermal Coupling Analysis to Identify Residue-Residue Interaction Networks that Facilitate Coupled-Domain Dynamics in Aminoacyl-tRNA Synthetases
(2012-04)
Aminoacyl-tRNA synthetases (ARSs) are multi-domain proteins that catalyze covalent
attachment of amino acids to the 3'-end of the cognate tRNA molecules. Long-range domain-domain
communications are known to play an ...
Comparison of Coarse-Grained and Atomistic-Level Simulations for Aminoacyl-tRNA Synthetases
(2013-05)
Aminoacyl-tRNA Synthetases are a group of multi-domain enzymes responsible for catalyzing the covalent attachment of an amino acid to its corresponding tRNA forming an aminoacyl-tRNA. A characteristic of AARSs is the large ...
Computational and Experimental Studies to Unravel the Role of Editing Domain of Bacterial Prolyl-tRNA Synthetases in Amino Acid Activation
(2012-04)
Prolyl-tRNA synthetases (ProRSs) are multi-domain proteins that catalyze covalent attachment of proline to the 3'-end of the tRNA[superscript]Pro. ProRSs from all three kingdoms of life are known to misactivate alanine and ...