Point mutants of elongation factor tu from e. coli impaired in binding aminoacyl-tRNA

机译：来自e的延伸因子tu的点突变体。结合氨酰-tRNA受损的大肠杆菌

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Protein engineering is a powerful technique, which can be used to establish the relationship between the structure and function of a protein. The protein engienering process is cyclic and runs through the following steps: design of substitution based on structural information, site-directed mutagenesis, expression and purifiication of mutant protein and finally a functional and structural characterisation.

机译：蛋白质工程是一种强大的技术，可用于建立蛋白质的结构与功能之间的关系。蛋白质工程化过程是循环的，并遵循以下步骤：基于结构信息设计取代，定点诱变，突变蛋白的表达和纯化以及最终的功能和结构表征。

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《NATO Advanced Research Workshop on RNA Biochemistry and Biotechnology Poznan, Poland October 10-17, 1998》|1998年|p.169-193|共25页
会议地点 Poznan(PL)
作者
C. R. Knudsen; F. Mansilla; G. N. Pedersen; B. F. C. Clark;
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正文语种 eng
中图分类生物化学;
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专利

1. Elongation Factor Ts Directly Facilitates the Formation and Disassembly of the Escherichia coli Elongation Factor Tu·GTP·Aminoacyl-tRNA Ternary Complex [J] . Benjamin Burnett, Roger Altman, Ryan Ferrao, The Journal of biological chemistry . 2013,第19期

机译：伸长因子TS直接促进大肠杆菌伸长因子TU·GTP·氨基酰基-TRNA三元复合物的形成和拆卸
2. Translation Elongation Factor 1A Mutants with Altered Actin Bundling Activity Show Reduced Aminoacyl-tRNA Binding and Alter Initiation via eIF2α Phosphorylation [J] . Winder Perez, Terri Goss Kinzy The Journal of biological chemistry . 2014,第30期

机译：翻译延伸因子1A肌动蛋白捆绑活性改变的突变体显示出降低的氨基酰基-TRNA结合和通过EIF2α磷酸化改变引发
3. Identification of the elongation factor Tu binding site on 70S E. coli ribosomes by chemical crosslinking [J] . Bishwajit Nag, Arthur E Johnson, Robert R Traut Indian Journal of Biochemistry & Biophysics . 1995,第6期

机译：通过化学交联鉴定70S大肠杆菌核糖体上的延伸因子Tu结合位点
4. Point mutants of elongation factor tu from e. coli impaired in binding aminoacyl-tRNA [C] . C. R. Knudsen, F. Mansilla, G. N. Pedersen, NATO advanced research workshop on RNA biochemistry and biotechnology . 1999

机译：从e的伸长因子Tu的点突变体。 Coli损害结合氨基酰基-TRNA
5. Structure-based design of mutant proteins: I. Molecular docking studies of amino acid binding to wild-type aminoacyl-tRNA synthetases. II. Structure-based design of mutant aminoacyl-tRNA synthetases for non-natural amino acid incorporation. [D] . Zhang, Deqiang. 2003

机译：基于结构的突变蛋白设计：I.氨基酸与野生型氨酰基tRNA合成酶结合的分子对接研究。二。非天然氨基酸掺入的突变型氨酰基-tRNA合成酶的基于结构的设计。
6. Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. [O] . T Pape, W Wintermeyer, M V Rodnina 1998

机译：伸长因子Tu依赖性的氨酰基tRNA与大肠杆菌核糖体A位点结合的完整动力学机制。
7. Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA [O] . Carsten ANDERSEN, Ove WIBORG 1994

机译：大肠杆菌伸长因子-u突变体，其对氨基酰基-TRNA的亲和力降低
8. Structural consequences of two methyl additions in the E. coli trp repressor L-tryptophan binding pocket [R] . Lawson, C. L. 1995

机译：在大肠杆菌trp阻遏物L-色氨酸结合口袋中添加两个甲基的结构后果

Point mutants of elongation factor tu from e. coli impaired in binding aminoacyl-tRNA

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