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Truncated elongation factor G lacking the G domain promotes translocation of the 3' end but not of the anticodon domain of peptidyl-tRNA.

The mechanism by which elongation factor G (EF-G) catalyzes the translocation of tRNAs and mRNA on the ribosome is not known. The reaction requires GTP, which is hydrolyzed to GDP. Here we show that EF-G from Escherichia coli lacking the G domain still catalyzed partial translocation in that it prom...

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書目詳細資料
發表在:Proc Natl Acad Sci U S A
Principais autores: Borowski, C, Rodnina, M V, Wintermeyer, W
格式: Artigo
語言:Inglês
出版: National Academy of Sciences 1996
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在線閱讀:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC39512/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8633041/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.9.4202
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