AbstractPhenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus can incorporate more than one molecule of phenylalanine into the tRNAPhe. It is shown that the ‘hyperaminoncylated’ tRNAPPhe is the bis-2′,3′-O-phenylalanyl-tRNAPhe, and its formation is typical for the thermophilic enzyme but does not occur for E. coli phenylalanyl-tRNA synthetase under the same conditions
AbstractAminoacyl-tRNA (AA-tRNA) formation is a key step in protein biosynthesis. This reaction is c...
SummaryAll class II aminoacyl-tRNA synthetases (aaRSs) are known to be active as functional homodime...
AbstractBackground: The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10...
AbstractPhenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus ca...
AbstractThe contribution of entire domains or particular amino acid residues of the phenylalanyl-tRN...
AbstractThe relationship between thermostability and functional activities of phenylalanyl-tRNA synt...
SummaryAminoacyl-tRNA synthetases exert control over the accuracy of translation by selective pairin...
AbstractBackground: In the translation of the genetic code each aminoacyl-tRNA synthetase (aaRS) mus...
Abstracts4U-containing transcripts of tRNAPhe gene have been prepared by complete substitution of 16...
AbstractPhenylalanyl-tRNA synthetase from Thermus thermophilus HB8 was isolated, characterized and c...
AbstractPhenylalanyl-tRNA synthetase from Escherichia coli does not catalyze the [14C]phenylalanyl r...
AbstractFPLC separation of α- and β-subunits of phenylalanyl-tRNA synthetases from E. coli MRE-600 a...
AbstractIt has previously been demonstrated that the unnatural amino acid p-Cl-phenylalanine can be ...
Aminoacyl-tRNA synthetase-containing complexes have been identified in different eukaryotes, and the...
AbstractMisacylated phenylalanyl-tRNALys, just as lysyl-tRNALys, but not phenylalanyl-tRNAPhe, have ...
AbstractAminoacyl-tRNA (AA-tRNA) formation is a key step in protein biosynthesis. This reaction is c...
SummaryAll class II aminoacyl-tRNA synthetases (aaRSs) are known to be active as functional homodime...
AbstractBackground: The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10...
AbstractPhenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus ca...
AbstractThe contribution of entire domains or particular amino acid residues of the phenylalanyl-tRN...
AbstractThe relationship between thermostability and functional activities of phenylalanyl-tRNA synt...
SummaryAminoacyl-tRNA synthetases exert control over the accuracy of translation by selective pairin...
AbstractBackground: In the translation of the genetic code each aminoacyl-tRNA synthetase (aaRS) mus...
Abstracts4U-containing transcripts of tRNAPhe gene have been prepared by complete substitution of 16...
AbstractPhenylalanyl-tRNA synthetase from Thermus thermophilus HB8 was isolated, characterized and c...
AbstractPhenylalanyl-tRNA synthetase from Escherichia coli does not catalyze the [14C]phenylalanyl r...
AbstractFPLC separation of α- and β-subunits of phenylalanyl-tRNA synthetases from E. coli MRE-600 a...
AbstractIt has previously been demonstrated that the unnatural amino acid p-Cl-phenylalanine can be ...
Aminoacyl-tRNA synthetase-containing complexes have been identified in different eukaryotes, and the...
AbstractMisacylated phenylalanyl-tRNALys, just as lysyl-tRNALys, but not phenylalanyl-tRNAPhe, have ...
AbstractAminoacyl-tRNA (AA-tRNA) formation is a key step in protein biosynthesis. This reaction is c...
SummaryAll class II aminoacyl-tRNA synthetases (aaRSs) are known to be active as functional homodime...
AbstractBackground: The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10...