ArticleScientific reports2017
Balance between hydration enthalpy and entropy is important for ice binding surfaces in Antifreeze Proteins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 36 citations in OpenAlex.
- Discovering naturally occurring antifreeze peptides from microbiome by integrating protein language models and molecular dynamics simulation.Journal of materials chemistry. B · 2026Article
- Adsorption Barrier Limits the Ice Inhibition Activity of Glycan-Rich Antifreeze Glycoproteins.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Quantum Chemical Microsolvation by Automated Water Placement.Molecules (Basel, Switzerland) · 2021Article
- The atomistic details of the ice recrystallisation inhibition activity of PVA.Nature communications · 2021Article
- Role of Displacing Confined Solvent in the Conformational Equilibrium of β-Cyclodextrin.The journal of physical chemistry. B · 2019Article
- Molecular Dynamics Gives New Insights into the Glucose Tolerance and Inhibition Mechanisms on β-Glucosidases.Molecules (Basel, Switzerland) · 2019Article
- Preordering of water is not needed for ice recognition by hyperactive antifreeze proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Antifreeze Proteins (AFPs) inhibit the growth of an ice crystal by binding to it. The detailed binding mechanism is, however, still not fully understood. We investigated three AFPs using Molecular Dynamics simulations in combination with Grid Inhomogeneous Solvation Theory, exploring their hydration thermodynamics. The observed enthalpic and entropic differences between the ice-binding sites and the inactive surface reveal key properties essential for proteins in order to bind ice: While entropic contributions are similar for all sites, the enthalpic gain for all ice-binding sites is lower than for the rest of the protein surface. In contrast to most of the recently published studies, our analyses show that enthalpic interactions are as important as an ice-like pre-ordering. Based on these observations, we propose a new, thermodynamically more refined mechanism of the ice recognition process showing that the appropriate balance between entropy and enthalpy facilitates ice-binding of proteins. Especially, high enthalpic interactions between the protein surface and water can hinder the ice-binding activity.
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