Stereochemistry and lifetime of the GTP hydrolysis intermediate at the active site of elongation factor Tu from Bacillus stearothermophilus as inferred from the 17O-55Mn superhyperfine interaction
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1990.tb15411.x/fullpdf
Reference30 articles.
1. 1. D. L. Miller, H. Weissbach, H. Weissbach, and S. Pestka (1977 ) inMolecular mechanism of protein biosynthesis () pp.332 -373 , Academic Press, New York.
2. Primary structure of elongation factor Tu from Escherichia coli.
3. Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins
4. Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.
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1. The Effect of pH and Various Cations on the GTP Hydrolysis of Rice Heterotrimeric G-protein α Subunit Expressed in Escherichia Coli;BMB Reports;2003-03-31
2. Ras Catalyzes GTP Hydrolysis by Shifting Negative Charges from γ- to β-Phosphate As Revealed by Time-Resolved FTIR Difference Spectroscopy;Biochemistry;2001-02-15
3. Time-Resolved FTIR Studies of the GTPase Reaction of H-Ras P21 Reveal a Key Role for the β-Phosphate;Biochemistry;1998-06-20
4. Low Affinity Interactions of GDPβS and Ribose- or Phosphoryl-substituted GTP Analogues with the Heterotrimeric G Protein, Transducin;Journal of Biological Chemistry;1996-05
5. Messenger RNA translation in prokaryotes: GTPase centers associated with translational factors;Biochimie;1996-01
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