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Keywords {🔍}

trna, doi, pubmed, google, scholar, eftu, pmc, amino, article, free, trnas, binding, anticodon, acids, acid, decoding, codon, biol, incorporation, sequence, function, ribosome, esterified, translation, body, mutations, uhlenbeck, rate, coli, stem, chem, bacterial, codonanticodon, recognition, species, structure, aatrna, protein, uaatrna, elongation, accuracy, modifications, uaas, mol, tuning, unnatural, efficient, multiple, formation, crystal,

Topics {✒️}

cys-trnacys-ef-tu-gdpnp reveals general binds ef-tu weakly thermus thermophilus ef-tu pmc beta search elongation factor tu-gtp escherichia coli aminoacyl-trnas spontaneous peptidyl-trna dissociation simpler ef-tu tuning unnatural l-aminoacyl-trnas inefficient ef-tu binding weaker codon-anticodon interaction increasing ef-tu concentration[18] ef-tu binding specificity ef-tu evolutionary tuning stable codon-anticodon interaction ef-tu binding affinity ef-tu binding data intrinsic codon-anticodon strength escherichia coli enhances ef-tu recognition region elongation factor tu transfer rna-mediated regulation bulky uaa-trna showed evaluating mistuned uaa-trnas ef-tu pocket mutations badly “mistuned” uaa-trna including elongation factor total free energy bind ef-tu coli trnaala shows codon-anticodon interactions resulting “mistuned” uaa-trna unnatural amino acid 70s ribosome complexed fully tuned uaa-trna peptide bond formation esterified amino acid amino acid fits license information pmcid outwitting ef-tu ef-tu fast ef-tu molecules ef-tu universal vary substantially due coli strains missing unnatural amino acids ef-tu mutations uag codon remains codon recognition requires codon recognition complicates

Questions {❓}

• Schrader JM, Uhlenbeck OC: Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?

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