Figure 6.
The S211F and H418R mutations alter GlyRS dimerization and the release kinetics of the cognate tRNAGly. (A), Size-exclusion chromatography of purified recombinant hGlyRS proteins. D:M, dimer-to-monomer ratio. (B), Kon and Koff values of tRNAGly-GCC binding and release, respectively, to the dimer form of the indicated hGlyRS variants. The percentage in parentheses denotes the frequency of a measured value.

The S211F and H418R mutations alter GlyRS dimerization and the release kinetics of the cognate tRNAGly. (A), Size-exclusion chromatography of purified recombinant hGlyRS proteins. D:M, dimer-to-monomer ratio. (B), Kon and Koff values of tRNAGly-GCC binding and release, respectively, to the dimer form of the indicated hGlyRS variants. The percentage in parentheses denotes the frequency of a measured value.

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