Magnetic resonance studies of the manganese guanosine di- and triphosphate complexes with elongation factor Tu.
Open Access
- 1 March 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (6) , 2004-2009
- https://doi.org/10.1016/s0021-9258(18)71856-5
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli W). I. Temperature and frequency dependent nuclear magnetic resonance studiesBiochemistry, 1976
- Nuclear magnetic resonance studies of protein-RNA interactions: I. The elongation factor Tu. GTP aminoacyl-tRNA complexJournal of Molecular Biology, 1974
- Binding of MnADP− to phosphoglycerate kinaseFEBS Letters, 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
- Antibiotic X‐5108. VI. Relative configuration of the tetrahydrofuran moiety of goldinamine. Preliminary communicationHelvetica Chimica Acta, 1974
- Antibiotic X-5108. V. Structures of antibiotic X-5108 and mocimycinJournal of the American Chemical Society, 1973
- Magnetic resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinaseBiochemistry, 1973
- Evidence for conformational changes in elongation factor Tu induced by GTP and GDPBiochemical and Biophysical Research Communications, 1973
- Peptide Chain Elongation: Discrimination against the Initiator Transfer RNA by Microbial Amino-acid Polymerization FactorsNature, 1968
- Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance ExperimentsPhysical Review B, 1954