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The glutaminyl-transfer RNA synthetase of Escherichia coli. Purification, structure and function relationship.
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Equilibrium measurements of cognate and noncognate interactions between aminoacyl transfer RNA synthetases and transfer RNA.
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Molecular weighr of Escherichia coli glutaminyl transfer ribonucleic acid synthetase, and isolation of its complex with glutamine transfer ribonucleic acid.
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Binding of transfer RNA and arginine to the arginine transfer RNA synthetase of Escherichia coli.
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A single mutational modification of a tryptophan-specific transfer RNA permits aminoacylation by glutamine and translation of the codon UAG.
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Amino acid acceptor stem of E. coli suppressor tRNA tyr is a site of synthetase recognition.
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Incorrect aminoacylatins catalysed by the phenylalanyl-and valyl-tRNA synthetases from yeast.
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Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase. Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation.
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Aminoacyl-tRNA synthetases: sone recent results and achievements.
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