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. 2024 Feb 2;7:147. doi: 10.1038/s42003-024-05842-1

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — Isothermal titration calorimetry (ITC) profiles corresponding to the binding of (i) ATP, (ii) ApCpp and (iii) cAMP to OaPAC. The upper panels show the raw data for the titration of nucleotides with OaPAC and the lower panels show the integrated heats of binding obtained from the raw data, after subtracting the heat of dilution. The solid lines in the lower panels represent the best fits to the experimental data, using the one set of sites model from the MicroCal PEAQ Analysis Software. No binding was observed for cAMP (iii). The binding signature plots (thermodynamic signatures; ΔG: blue, ΔH: green, -ΔTS: red) are also displayed for the binding events for ATP and ApCpp (inset in the lower panels).