AbstractAffinity labelling of E. coli ribosomes with the 2',3'-O-[4-(N-2-chloroethyl)-N-methylamino]benzylidene derivative of AUGU6 was studied within the initiation complex (complex I) obtained by using fMet-tRNAfMet and initiation factors and within the pretranslocational complex (complex II) obtained by treatment of complex I with the ternary complex Phe-tRNAPhe-GTP-EF-Tu. Both proteins and rRNA of 30 S as well as 50 S subunits were found to be labelled. Sets of proteins labelled within complexes I and II differ considerably. Within complex II, proteins S13 and L10 were labelled preferentially. On the other hand, within complex I, multiple modification is observed (proteins S4, S12, S13, S14, S15, S18, S19, S20/L26 were found to be alkyl...
Various aspects of protein synthesis have been studied, both to gain insight into its mechanism and ...
AbstractIn the figure, 30 S ribosomal proteins have been arranged according to their functional role...
AbstractNucleotide residues of E.coli tRNA interacting directly with proteins in pre- and posttransl...
AbstractAffinity labelling of E. coli ribosomes with the 2',3'-O-[4-(N-2-chloroethyl)-N-methylamino]...
AbstractPhotoreactive derivatives of E. coli tRNAPhe bearing arylazido groups on guanine residues (a...
AbstractrRNA-protein cross-links in free E. Coli35S-labeled 70 S ribosomes and in the initiation com...
AbstractAffinity labelling of E. coli ribosomes is performed by treatment with water-soluble carbodi...
International audienceIn this report, we have used periodate-oxidized tRNA (tRNAox) as an affinity la...
AbstractThe cleavable homobifunctional reagent dichloro[N,N,N′,N′-tetrakis(2-aminoethyl)-1,6-hexamet...
AbstractFrom the affinity labelling of 70 S ribosomes with a photoreactive derivative of Phe-tRNAphe...
To gain a better understanding of the architecture of the ribosome in general, and the structure of ...
*S Supporting Information ABSTRACT: The universally conserved translation elongation factor EF-Tu de...
AbstractAffinity labelling of pancreatic RNase with 4-(N-2-chloroethyl-N-methylamino)benzylamide and...
AbstractIn an attempt to understand how Escherichia coli ribosomes recognize the initiator codon on ...
The ribosome, a large ribonucleoprotein complex responsible for protein synthesis, has three or more...
Various aspects of protein synthesis have been studied, both to gain insight into its mechanism and ...
AbstractIn the figure, 30 S ribosomal proteins have been arranged according to their functional role...
AbstractNucleotide residues of E.coli tRNA interacting directly with proteins in pre- and posttransl...
AbstractAffinity labelling of E. coli ribosomes with the 2',3'-O-[4-(N-2-chloroethyl)-N-methylamino]...
AbstractPhotoreactive derivatives of E. coli tRNAPhe bearing arylazido groups on guanine residues (a...
AbstractrRNA-protein cross-links in free E. Coli35S-labeled 70 S ribosomes and in the initiation com...
AbstractAffinity labelling of E. coli ribosomes is performed by treatment with water-soluble carbodi...
International audienceIn this report, we have used periodate-oxidized tRNA (tRNAox) as an affinity la...
AbstractThe cleavable homobifunctional reagent dichloro[N,N,N′,N′-tetrakis(2-aminoethyl)-1,6-hexamet...
AbstractFrom the affinity labelling of 70 S ribosomes with a photoreactive derivative of Phe-tRNAphe...
To gain a better understanding of the architecture of the ribosome in general, and the structure of ...
*S Supporting Information ABSTRACT: The universally conserved translation elongation factor EF-Tu de...
AbstractAffinity labelling of pancreatic RNase with 4-(N-2-chloroethyl-N-methylamino)benzylamide and...
AbstractIn an attempt to understand how Escherichia coli ribosomes recognize the initiator codon on ...
The ribosome, a large ribonucleoprotein complex responsible for protein synthesis, has three or more...
Various aspects of protein synthesis have been studied, both to gain insight into its mechanism and ...
AbstractIn the figure, 30 S ribosomal proteins have been arranged according to their functional role...
AbstractNucleotide residues of E.coli tRNA interacting directly with proteins in pre- and posttransl...