Chemical modification studies of a protein at the peptidyltransferase site of the Bacillus stearothermophilus ribosome. The 50 S ribosomal subunit is a highly integrated functional unit.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference44 articles.
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1. Adsorption Mechanism of Ribosomal Protein L2 onto a Silica Surface: A Molecular Dynamics Simulation Study;Langmuir;2010-04-29
2. Reconstitution of Functional 50S Ribosomes from in Vitro Transcripts of Bacillus stearothermophilus 23S rRNA;Biochemistry;1999-01-16
3. Identification by site-directed mutagenesis of amino acid residues in ribosomal protein L2 that are essential for binding to 23S ribosomal RNA;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1998-12
4. Evidence for the participation of histidine residues located in the 56 kDa C-terminal polypeptide domain of ADP-ribosyl transferase in its catalytic activity;FEBS Letters;1990-10-29
5. Location of the binding region for 23S ribosomal RNA on ribosomal protein L2 from Bacillus stearothermophilus;European Journal of Biochemistry;1985-12
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