Single turnover kinetic studies of guanosine triphosphate hydrolysis and peptide formation in the elongation factor Tu-dependent binding of aminoacyl-tRNA to Escherichia coli ribosomes.
Open Access
- 1 December 1980
- journal article
- abstracts
- Published by Elsevier
- Vol. 255 (23) , 11088-11090
- https://doi.org/10.1016/s0021-9258(19)70256-7
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- A simple rapid mixing deviceAnalytical Biochemistry, 1980
- Kinetic analysis of the properties and reactions of enzymesProgress in Biophysics and Molecular Biology, 1976
- Kinetic Analysis of ATPase MechanismsQuarterly Reviews of Biophysics, 1976
- Content of elongation factor Tu in Escherichia coli.Proceedings of the National Academy of Sciences, 1975
- Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsinBiochemistry, 1973
- Efficiency of protein and messenger RNA synthesis in bacteriophage T4-infected cells of Escherichia coliJournal of Molecular Biology, 1972
- Growth rate of polypeptide chains as a function of the cell growth rate in a mutant of Escherichia coli 15Journal of Molecular Biology, 1971
- Further Studies on Bacterial Polypeptide ElongationPublished by Cold Spring Harbor Laboratory ,1969
- Peptide Chain ElongationCold Spring Harbor Symposia on Quantitative Biology, 1969
- RNA Codewords and Protein SynthesisScience, 1964