Browsing CERCA by Subject "Macromolecular crowding"
Now showing items 1-8 of 8
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Application of Spectroscopic Techniques to Study Molecular Crowding Effects on the Structure and Functions of Escherichia coli Prolyl-tRNA Synthetase
(2022-04)Many in vitro experiments with enzymes are performed in dilute conditions that do not resemble the cellular environment, which is crowded with various biomolecules. Crowding can impact an enzyme's structure, intrinsic ... -
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 ... -
Investigating the Effects of Molecular Crowding on Protein Structure using Atomic Force Microscopy
(2021-04)To explore the structure-dynamics-function relationship in proteins, most studies are usually conducted in simple salt-buffer solutions, however, the interior of a cell is densely crowded. The concentration of macromolecular ... -
Investigating the Effects of Molecular Crowding on Substrate- Binding using Isothermal Titration Calorimetry and STD-NMR
(2024-04)Conventional in vitro methods use buffers and salts to mimic the intracellular environment. However, by simplifying the in vivo environment, these methods lack essential structural elements that have been shown to impact ... -
Probing the Effects of Molecular Crowding on Protein Structure Using Atomic Force Microscopy
(2024-04)Enzymes exist in crowded cellular environments. However, conventionalin vitroandin silicoenzymatic studies are conducted in dilute conditions that do not consider the molecular crowding effects on an enzyme's structure and ... -
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 ... -
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 ...