Chemical evidence for the involvement of histidyl residues in the functioning of Escherichia coli elongation factor Tu
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(80)80937-9/fullpdf
Reference20 articles.
1. The role of guanosine 5′-triphosphate in polypeptide chain elongation
2. The binding site for the 3′-terminus of aminoacyl-tRNA in the molecule of elongation factor TufromEscherichia coli
3. Interaction of Escherichia coli EF-Tu . GTP and EF-Tu . GDP with Analogues of the 3' Terminus of Aminoacyl-tRNA
4. Amino acid sequences of two sulfhydryl-containing tryptic peptides of the polypeptide chain elongation factor Tu
Cited by 19 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Modification ofBacillus subtiliselongation factor Tu by N-tosyl-L phenylalanyl chloromethane abolishes its ability to interact with the 3′-terminal polynucleotide structure but not with the acyl bond in aminoacyl-tRNA;FEBS Letters;1989-07-17
2. Cross-linked amino acids in the protein pair S13-S19 and sequence analysis of protein S13 of Bacillus stearothermophilus ribosomes;Biochemistry;1988-05-03
3. Molecular properties of elongation factor Tu fromStreptomyces aureofaciens andEscherichia coli;Folia Microbiologica;1988-03
4. Reactivity of essential histidine residues in EF-Tu · GDP and EF-Tu · GTP from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1987-01
5. Structural homology between elongation factors EF - Tu from Bacillus stearothermophilus and Escherichia coli in the binding site for aminoacyl-tRNA;European Journal of Biochemistry;1986-01
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