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STOICHIOMETRY FOR THE ELONGATION-FACTOR TU AMINOACYL-TRANSFER-RNA COMPLEX SWITCHES WITH TEMPERATURE
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
1995 (English)In: BIOCHEMISTRY, ISSN 0006-2960, Vol. 34, no 3, 715-719 p.Article in journal (Other scientific) Published
Abstract [en]

In bacterial protein synthesis binding of an aminoacyl-transferRNA (aa-tRNA) to the ribosomal acceptor site (A-site) is catalyzed by elongation factor Tu (EF-Tu). Two guanosine triphosphates (GTPs) are hydrolyzed on EF-Tu for every bound aa-tRNA. This was

Place, publisher, year, edition, pages
AMER CHEMICAL SOC , 1995. Vol. 34, no 3, 715-719 p.
Keyword [en]
TRANSFER-RNA-BINDING; POLYPEPTIDE-CHAIN ELONGATION; CODON-ANTICODON INTERACTION; ESCHERICHIA-COLI; EF-TU; MOLECULES PARTICIPATE; RIBOSOMES; GTP; TRANSLATION; SEPARATION
Identifiers
URN: urn:nbn:se:uu:diva-80604OAI: oai:DiVA.org:uu-80604DiVA: diva2:108518
Note
Addresses: BILGIN N, UPPSALA UNIV, CTR BIOMED, DEPT BIOL MOLEC, BOX 590, S-75124 UPPSALA, SWEDEN.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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