Browsing CERCA by Author "Tadayon, Stephanie N."
Now showing items 1-4 of 4
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Application of Statistical-Thermal Coupling Analysis to Identify Residue-Residue Interaction Networks that Facilitate Coupled-Domain Dynamics in Aminoacyl-tRNA Synthetases
Lehman, Brent P.; Tadayon, Stephanie N.; Zirbes, Arrianna M.; Johnson, James Michael (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
Strom, Alexander M.; Yang, Yer; Tadayon, Stephanie N. (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 ... -
Comparison of Coarse-Grained and Atomistic-Level Simulations for Aminoacyl-tRNA Synthetases
Strom, Alexander M.; Tadayon, Stephanie N.; Yang, Yer (2012-04)Aminoacyl-tRNA synthetases (AARSs) are a group of multi-domain enzymes responsible for catalyzing the covalent attachment of an amino acid to the cognate tRNA forming an aminoacyl-tRNA. In this study, both atomistic-level ... -
Computational and Experimental Studies to Unravel the Role of Editing Domain of Bacterial Prolyl-tRNA Synthetases in Amino Acid Activation
Tadayon, Stephanie N.; Zirbes, Arrianna M.; Johnson, James Michael; Strom, Alexander M.; Lehman, Brent P. (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 ...