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. 2021 Oct 28;49(20):11653–11665. doi: 10.1093/nar/gkab942

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 4. — Fitting telomerase inhibition data. (A) Schema of competitive binding mechanism and relevant equilibrium equations. (B) Best fit telomerase inhibition curves. Telomerase inhibition assay data (points) were corrected by a factor of 3 relative to those in Supplementary Figure S2, as described in Materials and Methods. The predicted fraction bound curves were generated with optimized and γ values of 0.324 nM and 0.465, respectively. Inhibition by WT CST. (C) Heat map of error values. Error values (residual Sum of squares, see Materials and Methods) as a function of γ and K_d telomerase–DNA pairs with pair of best fit indicated. Value of error colored per bar on right.

Inline graphic — Fitting telomerase inhibition data. (A) Schema of competitive binding mechanism and relevant equilibrium equations. (B) Best fit telomerase inhibition curves. Telomerase inhibition assay data (points) were corrected by a factor of 3 relative to those in Supplementary Figure S2, as described in Materials and Methods. The predicted fraction bound curves were generated with optimized and γ values of 0.324 nM and 0.465, respectively. Inhibition by WT CST. (C) Heat map of error values. Error values (residual Sum of squares, see Materials and Methods) as a function of γ and K_d telomerase–DNA pairs with pair of best fit indicated. Value of error colored per bar on right.