The "allosteric three-site model" of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 22, 1996, Pages 12183-12188

  Semenkov, Yuri P ^a   Rodnina, Marina V ^b   Wintermeyer, Wolfgang ^b  

^a PETERSBURG NUCLEAR PHYSICS INSTITUTE   (Russian Federation)

^b UNIVERSITY OF WITTEN HERDECKE   (Germany)

Author keywords

Elongation factor G; Exit site; Protein synthesis; Translocation

Indexed keywords

ELONGATION FACTOR G; MESSENGER RNA; TRANSFER RNA;

CONFERENCE PAPER; CONTROLLED STUDY; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; RIBOSOME; RNA TRANSLATION; TRANSLATION REGULATION;

ALLOSTERIC REGULATION; ESCHERICHIA COLI; MAGNESIUM; MODELS, MOLECULAR; PEPTIDE CHAIN ELONGATION, TRANSLATIONAL; PEPTIDE ELONGATION FACTOR G; PEPTIDE ELONGATION FACTORS; POLYAMINES; PROTEIN BIOSYNTHESIS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RIBOSOMES; RNA, TRANSFER, AMINO ACYL; RNA, TRANSFER, MET;

ESCHERICHIA COLI;

EID: 0029959815     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.22.12183     Document Type: Article

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