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. 2020 May 26;11:2644. doi: 10.1038/s41467-020-16341-2

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© The Author(s) 2020

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. 6 — a Fit of the two-state dead-end model to the calculated values of k_cat for the psychrophilic enzyme and (b) the corresponding fit of the heat capacity model to the same data points. Predictions of the two-state (c) and heat capacity (d) models of the temperature dependence of the apparent activation enthalpy and entropy contributions to the free energy barrier.