Abstract
Translational diffusion coefficients have been simulated for various conformations of tRNAPhe (yeast) by bead models, in order to analyze data obtained by dynamic light scattering on the free and the aminoacylated form. The 18% increase of the translational diffusion coefficient upon deacylation, reported by Potts et al. (1981), could not be represented by any change of the L-hinge angle, but could only be simulated by a conformation change to an extended form with extensive dissociation of base pairs. Since extensive unpairing is not consistent with evidence accumulated in the literature, the change of the diffusion coefficient must be mainly due to processes other than intramolecular conformational changes.
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Antosiewicz, J., Porschke, D. Effect of aminoacylation on tRNA conformation. Eur Biophys J 17, 233–235 (1989). https://doi.org/10.1007/BF00284730
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DOI: https://doi.org/10.1007/BF00284730