The N‐Terminal Sequence Protein of L7/L12 Is Responsible for Its Dimerization
- 1 October 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 90 (2), 309-312
- https://doi.org/10.1111/j.1432-1033.1978.tb12605.x
Abstract
Ultracentrifuge studies of intact protein L7/L12 [of Escherichia coli], of its fragments 27-120, 1-74 and 74-120 and of protein L7/L12 with oxidized methionine residues, indicate that the N[amino]-terminal sequence of the protein L7/L12 is responsible for its dimerization. The symmetry model of the dimer is discussed.This publication has 10 references indexed in Scilit:
- Dimer State of Protein L7/L12 and EF‐G‐Dependent Reactions on RibosomesEuropean Journal of Biochemistry, 1978
- Inhibition of EF-G dependent GTPase by an aminoterminal fragment of L7L/12Biochemical and Biophysical Research Communications, 1975
- Selective separation procedure for determination of ribosomal proteins L7 and L12Analytical Biochemistry, 1975
- Ribosomal protein neighborhoodsMolecular Genetics and Genomics, 1974
- The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solventsBiopolymers, 1973
- Prediction of the secondary structure of the L7, L12 proteins of the E. coli ribosomeFEBS Letters, 1973
- Amino acid sequence of a 50 S ribosomal protein involved in both EFG and EFT dependent GTP‐hydrolysisFEBS Letters, 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
- Immunochemistry of sperm whale myoglobin. IV. Role of the arginine residues in the conformation and differentiation of their roles in the antigenic reactivityBiochemistry, 1969
- [55] Oxidation with hydrogen peroxidePublished by Elsevier ,1967