ArticleProtein science : a publication of the Protein Society2004
Theoretical study of interaction of winter flounder antifreeze protein with ice.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 103 citations in OpenAlex.
- An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- From freezing to functioning: cellular strategies of cold-adapted bacteria for surviving in extreme environments.Archives of microbiology · 2024Review
- How Can Ice Emerge at 0 °C?Biomolecules · 2022Article
- Mechanistic elucidation of freezing-induced surface decomposition of aluminum oxyhydroxide adjuvant.iScience · 2022Article
- Effects of Winter Flounder Antifreeze Protein on the Growth of Ice Particles in an Ice Slurry Flow in Mini-Channels.Biomolecules · 2019Article
- 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
- An Effective Antifreeze Protein Predictor with Ensemble Classifiers and Comprehensive Sequence Descriptors.International journal of molecular sciences · 2015Article
- The biological function of an insect antifreeze protein simulated by molecular dynamics.eLife · 2015Article
- 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
- Biomolecular electrostatics and solvation: a computational perspective.Quarterly reviews of biophysics · 2012Review
- 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
- Docking flexible ligands in proteins with a solvent exposure- and distance-dependent dielectric function.Journal of computer-aided molecular design · 2010Article
- Electro-optical properties characterization of fish type III antifreeze protein.Journal of biological physics · 2007Article
- Antifreeze proteins at the ice/water interface: three calculated discriminating properties for orientation of type I proteins.Biophysical journal · 2007Article
- Fluorescence microscopy evidence for quasi-permanent attachment of antifreeze proteins to ice surfaces.Biophysical journal · 2007Article
- Protein-solvent interactions.Chemical reviews · 2006Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antifreeze proteins (AFPs) are synthesized by various organisms to enable their cells to survive subzero environment. These proteins bind to small ice crystals and inhibit their growth, which if left uncontrolled would be fatal to cells. The crystal structures of a number of AFPs have been determined; however, crystallographic analysis of AFP-ice complex is nearly impossible. Molecular modeling studies of AFPs' interaction with ice surface is therefore invaluable. Early models of AFP-ice interaction suggested H-bond as the primary driving force behind such interaction. Recent experimental evidence, however, suggested that hydrophobic interactions could be the main contributor to AFP-ice association. All computational studies published to date were carried out to verify the H-bond model, and no works attempting to verify the hydrophobic interaction model have been published. In this work, we Monte Carlo-minimized complexes of several AFPs with ice taking into account nonbonded interactions, H-bonds, and the hydration potential for proteins. Parameters of the hydration potential for ice were developed with the assumption that the free energy of the water-ice association should be close to zero at equilibrium melting temperature. Our calculations demonstrate that desolvation of hydrophobic groups in the AFPs upon their binding to the grooves at the ice surface is indeed the major stabilizing contributor to the free energy of AFP-ice binding. This study is consistent with available structural and mutation data on AFPs. In particular, it explains the paradoxical finding that substitution of Thr residues with Val does not affect the potency of winter flounder AFP whereas substitution with Ser abolished its antifreeze activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.