Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
about
Synthetic biology challenges long-held hypotheses in translation, codon bias and transcription.Optimal codon choice can improve the efficiency and fidelity of N-methyl amino acid incorporation into peptides by in-vitro translation.Genetically encoded libraries of nonstandard peptides.Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome.In vivo incorporation of multiple noncanonical amino acids into proteins.A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acidsTranslational roles of the C75 2'OH in an in vitro tRNA transcript at the ribosomal A, P and E sites.The ribosome meets synthetic biology.
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P2860
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 17 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@en
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@nl
type
label
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@en
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@nl
prefLabel
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@en
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@nl
P2860
P356
P1476
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
@en
P2093
Anthony C Forster
P2860
P304
P356
10.1093/NAR/GKP240
P407
P577
2009-04-17T00:00:00Z