Structural homology between elongation factors EF - Tu from Bacillus stearothermophilus and Escherichia coli in the binding site for aminoacyl-tRNA
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1986.tb09405.x/fullpdf
Reference25 articles.
1. The Elongation Factor EF-Tu and Its Two Encoding Genes
2. Primary structure of elongation factor Tu from Escherichia coli.
3. The Complete Amino-Acid Sequence of Elongation Factor Tu from Escherichia coli
4. The binding site for the 3′-terminus of aminoacyl-tRNA in the molecule of elongation factor TufromEscherichia coli
5. Interaction of Escherichia coli EF-Tu . GTP and EF-Tu . GDP with Analogues of the 3' Terminus of Aminoacyl-tRNA
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1. Recognition of Aminoacyl-tRNAs by Protein Elongation Factors;tRNA;2014-04-30
2. Bacterial elongation factors EF-Tu, their mutants, chimeric forms, and domains: Isolation and purification;Journal of Chromatography B;2007-04
3. Thermostability of multidomain proteins: Elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms;Protein Science;2004-01-01
4. Cloning and Characterization of the str Operon and Elongation Factor Tu Expression in Bacillus stearothermophilus;Journal of Bacteriology;2000-11
5. Structure and expression of elongation factor tu from Bacillus stearothermophilus 1 1Edited by D. Draper;Journal of Molecular Biology;1998-10
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