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. 2018 Jan;24(1):56–66. doi: 10.1261/rna.062893.117

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© 2018 McKenney et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 6. — Kinetic determination of dissociation constant of TbTrm140 to tRNA^Thr in the presence of TbADAT2/3. (A) Single turnover assays of TbTrm140 to tRNA^Thr_CGU in the presence of TbADAT2/3 were performed as described in Materials and Methods. The fraction of methylated cytosine 32 was measured for each TbTrm140 protein concentration ranging from 10 to 2500 nM as shown in the graph. The methylated fraction was plotted as a function of time and fit to a single exponential curve [f = a(1 − e^−kt)], where f represents methylated cytosine formed, a denotes methylated cytosine produced at the end point of the reaction, k signifies k_obs, and t is time. (B) The resulting k_obs values were plotted against the concentration of TbTrm140 and fit to a single ligand binding isotherm. The K_dapp was then determined by nonlinear regression using Sigmaplot. Each graph represents at least five independent replicates.