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 ...

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 ...

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 ...

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 ...

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 ...

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 ...

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, ...

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, ...

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 ...