Search
Now showing items 1-4 of 4
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 ...
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 ...
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 ...