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. 2019 Oct 21;9:15076. doi: 10.1038/s41598-019-50701-3

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© The Author(s) 2019

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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Binding energetics of Late domain peptides to hNEDD4-WW3. (a) Calorimetric titrations of peptide ligands into the hNEDD4-WW3 domain. Upper panels show the heat effects associated with the injection of each ligand into the calorimetric cell containing the hNEDD4-WW3 domain (1) and the dilution experiment of each ligand into the corresponding buffer under the same conditions and identical injection profile (2). The dilution curve has been displaced in the y-axis for representation purposes. Lower panels show the binding isotherm (open symbols) together with the best fit (continuous lines) to an appropriate binding model (see Methods for details). (b) Thermodynamic dissection of the binding energetics. Shown is the binding Gibbs energy (black bars) as well as the enthalpic (green bars) and entropic (blue bars) contributions. All parameters were determined at 25 °C in 20 mM sodium phosphate pH 7.0.