On the Structure, Function, and Dynamics of L7/L12 from Escherichia coliRibosomes
- 1 January 1986
- book chapter
- Published by Springer Nature
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- The L7/L12 proteins change their conformation upon interaction of EF‐G with ribosomesFEBS Letters, 1984
- The L7/L12 stalk, a conserved feature of the prokaryotic ribosome, is attached to the large subunit through its N terminusJournal of Molecular Biology, 1981
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- Identification of proteins located in the neighbourhood of the binding site for the elongation factor EF‐Tu on Escherichia coli ribosomesFEBS Letters, 1976
- Inhibition of EF-G dependent GTPase by an aminoterminal fragment of L7L/12Biochemical and Biophysical Research Communications, 1975
- The involvement of 50S ribosomal protein L11 in the EF‐G dependent GTP hydrolysis of E. coli ribosomesFEBS Letters, 1975
- Shape properties of proteins L7 and L12 from E. coli ribosomesBiochemical and Biophysical Research Communications, 1974
- Involvement of 50S ribosomal proteins L6 and L10 in the ribosome dependent GTPase activity of elongation factor GBiochemical and Biophysical Research Communications, 1973
- 50-S Ribsomal Proteins. Peptide Studies on Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coliEuropean Journal of Biochemistry, 1972
- 50-S Ribosomal Proteins. Purification and Partial Characterization of Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coliEuropean Journal of Biochemistry, 1972