Probing electrostatic interactions and ligand binding in aspartyl-tRNA synthetase through site-directed mutagenesis and computer simulations

Proteins: Structure, Function and Genetics

Volumn 71, Issue 3, 2008, Pages 1450-1460

  Thompson, Damien ^a,c   Lazennec, Christine ^b   Plateau, Pierre ^b   Simonson, Thomas ^b  

^a UNIVERSITY COLLEGE CORK   (Ireland)

^b LABORATOIRE DE BIOCHIMIE   (France)

^c NONE   (Ireland)

Author keywords

Aminoacyl tRNA synthetase; Free energy calculations; Kinetic binding assays; Ligand protein binding; Molecular dynamics simulations; Molecular recognition; Protein electrostatics; Protein engineering

Indexed keywords

ASPARAGINE; ASPARTATE TRANSFER RNA LIGASE; ASPARTIC ACID; GLUTAMINE; GLYCINE; HISTIDINE; LEUCINE; LYSINE; MUTANT PROTEIN; PYROPHOSPHATE;

ADENYLATION; ARTICLE; BIOENGINEERING; COMPUTER SIMULATION; CONFORMATION; ELECTRICITY; ENERGY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; EXPERIMENTATION; LIGAND BINDING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; SURFACE CHARGE;

ASPARTATE-TRNA LIGASE; BINDING SITES; COMPUTER SIMULATION; ELECTROSTATICS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING;

ESCHERICHIA COLI;

EID: 42449089814     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21834     Document Type: Article

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