Further Studies on the Properties of the Polypeptide Chain Elongation Factors Tu and Ts: Hydrogen-Tritium Exchange, Optical Rotatory Dispersion, and Intrinsic Fluorescence

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Abstract
The conformation and conformational stability of the polypeptide chain elongation factors Tu (EF-Tu) and Ts (EF-Ts) have been investigated by means of hydrogen-tritium exchange, optical rotatory dispersion and fluorescence spectroscopy, and the following results were obtained. These results indicate that the binding of GDP or GTP causes a gross conformational change in EF-Tu, stabilizing its secondary and tertiary structure, increasing its α-helical content, and reducing the motility of the protein core. The shielding of tryptophan fluorescence is more marked in EF-Tu·GDP than in EF-Tu·GTP, indicating that the conformations of these two forms of EF-Tu are different.