Pages that link to "Q69361642"

The following pages link to Studies on the polypeptide elongation factors form E. coli. VI. Characterization of sulfhydryl groups in EF-Tu and EF-Ts (Q69361642):

Displaying 29 items.

• Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography (Q27728967) (← links)
• The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution (Q27730883) (← links)
• The GTPase superfamily: conserved structure and molecular mechanism (Q27860524) (← links)
• The role of guanosine 5′-triphosphate in polypeptide chain elongation (Q28324529) (← links)
• GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site (Q35613520) (← links)
• Primary structure of elongation factor Tu from Escherichia coli (Q36359244) (← links)
• Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae (Q36602230) (← links)
• Design and properties of efficient tRNA:EF-Tu FRET system for studies of ribosomal translation (Q36778946) (← links)
• Studies on Polypeptide-Chain-Elongation Factors from an Extreme Thermophile, Thermus thermophilus HB8. 3. Molecular Properties (Q39233019) (← links)
• Inactivation of Escherichia coli elongation factor Ts by the arginine-specific reagent butanedione (Q39239312) (← links)
• Structural studies of ribosomes (Q40089160) (← links)
• Magnetic resonance studies of interactions of spin-labeled elongation factor Tu with ligands (Q40159998) (← links)
• Action of crystalline acid carboxypeptidase from Penicillium janthinellum (Q40337269) (← links)
• Reactivity of amino groups in various complexes of the peptide chain elongation factor EF-Tu from Escherichia coli a new method of competitive labelling using reductive methylation (Q40957778) (← links)
• Studies on Polypeptide-Chain-Elongation Factors from an Extreme Thermophile, Thermus thermophilus HB8. 2. Catalytic Properties (Q40991476) (← links)
• The binding site for the 3′-terminus of aminoacyl-tRNA in the molecule of elongation factor TufromEscherichia coli (Q41005159) (← links)
• The elongation factor Tu.kirromycin complex has two binding sites for tRNA molecules. (Q41314862) (← links)
• The Effect of Mg2+ on Some Properties of Nucleotide-Free Elongation Factor Tu from Bacillus stearothermophilus (Q41554305) (← links)
• Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21. (Q41562639) (← links)
• A sulphydryl group is not essential for the binding of GDP to elongation factor Tu (Q41623084) (← links)
• Functional interaction between bases C1049 in domain II and G2751 in domain VI of 23S rRNA in Escherichia coli ribosomes (Q41869920) (← links)
• Molecular properties of elongation factor Tu from Streptomyces aureofaciens and Escherichia coli (Q41892423) (← links)
• Amino acid sequence of elongation factor Tu. Sequence of a region containing the thiol group essential for GTP binding (Q44194547) (← links)
• Enzymatic properties of an acid carboxypeptidase from Aspergillus niger var. macrosporus (Q46145449) (← links)
• Amino acid sequences of two sulfhydryl-containing tryptic peptides of the polypeptide chain elongation factor Tu (Q66900994) (← links)
• Amino acid sequence of elongation factor Tu. Characterization and alignment of the cyanogen bromide fragments and location of the cysteine residues (Q67012877) (← links)
• Localization of possible functional domains in sup2 gene product of the yeast Saccharomyces cerevisiae (Q68957419) (← links)
• Identification of the N-tosyl-L-phenylalanyl chloromethylketone modification site in Thermus thermophilus elongation factor Tu (Q69384788) (← links)
• N-Tosyl-L-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tu from Escherichia coli (Q71476853) (← links)