ライフサイエンスコーパス: Phe-tRNA

コーパス検索結果 (left1)

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1 Binding of the ternary complex [14C]Phe-tRNA-elongation factor Tu.guanyl-5'-yl imidodiphosph

2 .guanyl-5'-yl imidodiphosphate) but not [14C]Phe-tRNA.elongation factor Tu.GDP.kirromycin increased l

3 is synthesized for every approximately 7,300 Phe-tRNA(Phe), compatible with an error rate in translat

4 the presence of deacyl-tRNA(Phe) or N-acetyl-Phe-tRNA(Phe) using poly(U) or an mRNA analogue containi

5 For N-acetyl-Phe-tRNA(Phe) with either poly(U) or the mRNA analogue,

6 esence of a peptidyl tRNA analogue, N-acetyl-Phe-tRNA(Phe), in the A site, which mimicked the post-pe

7 Binding of N-acetylated Phe-tRNA(Phe), an analog of the initiator fMet-tRNA(Met)

8 some bound with ternary complexes containing Phe-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI).

9 formation and dissociation of the EF-Tu-GTP-Phe-tRNA(Phe) ternary complex.

10 ant has a reduced affinity for mitochondrial Phe-tRNA(Phe).

11 active in polymerization with mitochondrial Phe-tRNA(Phe), this variant has low activity in the form

12 and slow phases similar to those for natural Phe-tRNA(Phe).

13 his tRNA, but still 2-fold less than natural Phe-tRNA(Phe).

14 conserved G37, adjacent to the anticodon of Phe tRNAs.

15 conserved base pairs in the tertiary core of Phe-tRNA(Phe), 18-55 and 19-56, on rate and equilibrium

16 s on the side chain of the esterified Phe of Phe-tRNA(Phe).

17 elongation as measured by polymerization of Phe-tRNA on a poly(U) template in presence of GDP can be

18 ues within the editing site had no effect on Phe-tRNA(Phe) synthesis, but abolished hydrolysis of Tyr

19 rameric protein responsible for synthesizing Phe-tRNA(Phe) during protein synthesis.

20 With a single exception (tRNA(Phe)-tRNA(Glu) pair), the parallelism is especially impr

21 rce in complexes carrying an aminoacyl tRNA, Phe-tRNA(Phe), in the A site, indicating that the SD int

22 upture force as compared to the complex with Phe-tRNA(Phe), and the resultant force was the same for

23 e affinities of the mutant proteins to yeast Phe-tRNA(Phe) determined.

24 do]triphosphate (EF-Tu.GDPNP) bound to yeast Phe-tRNA(Phe) reveals that EF-Tu interacts with the tRNA

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