The properties of the complex between ribosomal protein L2 and tRNA
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(85)81299-0/fullpdf
Reference22 articles.
1. The assembly of the prokaryotic ribosome
2. Polynucleotide-protein interactions in the translation system. Identification of proteins interacting with tRNA in the A- and P-sites of E. coli ribosomes
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1. Reconstitution of the 50S Subunit with In Vitro-Transcribed 23S rRNA: a New Tool for Studying Peptidyltransferase;The Ribosome;2014-04-08
2. Protein Kinase Associated with Ribosomes Phosphorylates Ribosomal Proteins ofStreptomyces collinus;Biochemical and Biophysical Research Communications;1997-09
3. Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity;Biochemistry and Cell Biology;1995-12-01
4. The complex between ribosomal proteins and animoacyl-tRNA: the interactions and hydrolytic activities are not confined to the proteins L2 and L16 of Escherichia coli ribosomes;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1990-04
5. The peptidyltransferase centre of the Escherichia coli ribosome. The histidine of protein L16 affects the reconstitution and control of the active centre but is not essential for release-factor-mediated peptidyl-tRNA hydrolysis and peptide bond formation;European Journal of Biochemistry;1987-06
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