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. 2017 Sep 19;7:11901. doi: 10.1038/s41598-017-11982-8

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© The Author(s) 2017

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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Schematic representation of the ice-binding process highlighting the influence of enthalpic interactions between the protein and the first hydration shell. Pre-ordering of the water molecules in an ice-like structure around the IBS (left); if the protein water interactions are too strong, the water molecules cannot rearrange and an energetically unfavorable mismatch between the ice and the protein occurs (bottom right). If the enthalpic interactions are weak, the springs are flexible and the water molecules are able to rearrange and fit to the ice lattice (top right).