Involvement of histidine residues in the substrate binding of elongation factor Tu from Thermus thermophilus: Proton nuclear magnetic resonance and photooxidation study
- 1 August 1979
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 196 (1) , 233-238
- https://doi.org/10.1016/0003-9861(79)90571-x
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
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- Studies on Polypeptide‐Chain‐Elongation Factors from an Extreme Thermophile, Thermus thermophilus HB8European Journal of Biochemistry, 1978
- High resolution X-ray crystallographic analysis of a modified form of the elongation factor Tu:Guanosine diphosphate complexJournal of Molecular Biology, 1978
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
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- Structural Fluctuation of the Polypeptide-Chain Elongation Factor Tu. A Comparison of Factors from Escherichia coli and Thermus thermophilus HB8European Journal of Biochemistry, 1977
- Conformational Transitions of Polypeptide Chain Elongation Factor Tu. II. Further Studies by Electron Spin ResonanceThe Journal of Biochemistry, 1976
- 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
- Studies on Polypeptide Elongation Factors from Escherichia coliPublished by Elsevier ,1972