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. 2018 Jan 12;8:689. doi: 10.1038/s41598-017-18733-9

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© The Author(s) 2018

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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Affinity and thermodynamics for trypsin analysed through SPR. SPR based thermodynamic analysis of MP-4-trypsin interaction at equilibrium. (a) Typical sensorgram for MP-4 and trypsin interaction at various concentrations. (b) K_D versus temperature. (c) Natural log of K_D versus inverse of temperature, slope indicate the Arrhenius values. (d) Individual contributions of enthalpy (ΔH) and entropy (TΔS) to equilibrium free energy of binding (ΔG), at temperatures ranging from 15° to 35 °C.