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Figure 8 | Biology Direct

Figure 8

From: Automated mass action model space generation and analysis methods for two-reactant combinatorially complex equilibriums: An analysis of ATP-induced ribonucleotide reductase R1 hexamerization data

Figure 8

Top 3 fits to the data of Kashlan et al. [20]. A) Fits of the top 3 models. The second model uses its dimer term to capture a slight downturn in average mass at high [ATP] (see Fig. 9), consistent with its geometric mean binding constant being greater than that of the hexamer term in Table 1. Not shown in this plot is the point (0 μM, 90 kDa) which all models fit perfectly if M1 = 90 is fixed (as it is here) rather than estimated. B) Residuals of the top model R6X8. The reduced variance and positive mean of the first 4 residuals may be due to bias arising from prior knowledge that the monomer is 90 kDa and thus too prior knowledge that the average mass must increase from 90 kDa. Non-weighted least squares gives less weight to these 4 points which, coincidentally, is advantageous given these suspicions. PlotDigitizer (Methods) was used to obtain the data from a pdf of the original paper, and as this step involves human intervention, it too may have introduced some bias and random error.

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