ArticleBiophysical journal2007
Antifreeze proteins at the ice/water interface: three calculated discriminating properties for orientation of type I proteins.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 99 citations in OpenAlex.
- Antifreeze Protein for Freeze-Thaw Durability Enhancement of Cement Mortar: Effects and Action Analysis.Materials (Basel, Switzerland) · 2026Article
- Discovering naturally occurring antifreeze peptides from microbiome by integrating protein language models and molecular dynamics simulation.Journal of materials chemistry. B · 2026Article
- Structures, dynamics, and hydrogen-bond interactions of antifreeze proteins in TIP4P/Ice water and their dependence on force fields.PloS one · 2018Article
- Balance between hydration enthalpy and entropy is important for ice binding surfaces in Antifreeze Proteins.Scientific reports · 2017Article
- Investigation of changes in structure and thermodynamic of spruce budworm antifreeze protein under subfreezing temperature.Scientific reports · 2017Article
- Neofunctionalization of zona pellucida proteins enhances freeze-prevention in the eggs of Antarctic notothenioids.Nature communications · 2016Article
- Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The biological function of an insect antifreeze protein simulated by molecular dynamics.eLife · 2015Article
- Antifreeze protein-induced selective crystallization of a new thermodynamically and kinetically less preferred molecular crystal.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013Article
- Antifreeze peptides and glycopeptides, and their derivatives: potential uses in biotechnology.Marine drugs · 2013Review
- Microfluidic experiments reveal that antifreeze proteins bound to ice crystals suffice to prevent their growth.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Thermodynamic Analysis of Thermal Hysteresis: Mechanistic Insights into Biological Antifreezes.The Journal of chemical thermodynamics · 2012Article
- Anchored clathrate waters bind antifreeze proteins to ice.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- Superheating of ice crystals in antifreeze protein solutions.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Solution- and adsorbed-state structural ensembles predicted for the statherin-hydroxyapatite system.Biophysical journal · 2009Article
- Direct visualization of spruce budworm antifreeze protein interacting with ice crystals: basal plane affinity confers hyperactivity.Biophysical journal · 2008Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antifreeze proteins (AFPs) protect many plants and organisms from freezing in low temperatures. Of the different AFPs, the most studied AFP Type I from winter flounder is used in the current computational studies to gain molecular insight into its adsorption at the ice/water interface. Employing molecular dynamics simulations, we calculate the free energy difference between the hydrophilic and hydrophobic faces of the protein interacting with ice. Furthermore, we identify three properties of Type I "antifreeze" proteins that discriminate among these two orientations of the protein at the ice/water interface. The three properties are: the "surface area" of the protein; a measure of the interaction of the protein with neighboring water molecules as determined by the number of hydrogen bond count, for example; and the side-chain orientation angles of the threonine residues. All three discriminants are consistent with our free energy results, which clearly show that the hydrophilic protein face orientations toward the ice/water interface, as hypothesized from experimental and ice/vacuum simulations, are incorrect and support the hypothesis that the hydrophobic face is oriented toward the ice/water interface. The adsorption free energy is calculated to be 2-3 kJ/mol.
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