Nuclear magnetic resonance studies of protein-RNA interactions: I. The elongation factor Tu. GTP aminoacyl-tRNA complex
Authors:
- 15 December 1974
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 90 (3) , 601-607
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNAJournal of Molecular Biology, 1974
- High-resolution nuclear magnetic resonance studies of the structure of transfer ribonucleic acid and other polynucleotides in solutionAccounts of Chemical Research, 1974
- Guanosine triphosphate and guanosine diphosphate as conformation-determining molecules. Differential interaction of a fluorescent probe with the guanosine nucleotide complexes of bacterial elongation factor TuBiochemistry, 1974
- [22] Elongation factor Tu and the aminoacyl-tRNA · EFTu · GTP complex1974
- Evidence for conformational changes in elongation factor Tu induced by GTP and GDPBiochemical and Biophysical Research Communications, 1973
- Investigation of exchangeable protons and the extent of base pairings in yeast phenylalanine transfer RNA by high resolution nuclear magnetic resonanceJournal of Molecular Biology, 1972
- Protein BiosynthesisAnnual Review of Biochemistry, 1971
- Nuclear magnetic resonance study of cyanoferrimyoglobin; Identification of pseudocontact shiftsJournal of Molecular Biology, 1970
- Proton NMR studies of hemoglobin in H2OBiochemical and Biophysical Research Communications, 1970
- Evidence for a guanine nucleotide-aminoacyl-RNA complex as an intermediate in the enzymatic transfer of aminoacyl-RNA to ribosomesBiochemical and Biophysical Research Communications, 1967