ArticleJournal of the Royal Society, Interface2014
Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics.
Article in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 91 citations in OpenAlex.
- How to measure the activity of antifreeze proteins?Biophysical reviews · 2025Review
- On the engulfment of antifreeze proteins by ice.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Extended Temperature Range of the Ice-Binding Protein Activity.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- The Nanoliter Osmometer: Thermal Hysteresis Measurement.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Divergent Mechanisms of Ice Growth Inhibition by Antifreeze Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Investigating the Interaction Between Ice-Binding Proteins and Ice Surfaces Using Microfluidic Devices and Cold Stages.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Nanoscopy of single antifreeze proteins reveals that reversible ice binding is sufficient for ice recrystallization inhibition but not thermal hysteresis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Intracellular and Extracellular Antifreeze Protein Significantly Improves Mammalian Cell Cryopreservation.Biomolecules · 2022Article
- A brief review of applications of antifreeze proteins in cryopreservation and metabolic genetic engineering.3 Biotech · 2019Review
- Ice-binding proteins and the applicability and limitations of the kinetic pinning model.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019Article
- The physics and chemistry of ice.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019Article
- Structures, dynamics, and hydrogen-bond interactions of antifreeze proteins in TIP4P/Ice water and their dependence on force fields.PloS one · 2018Article
- From ice-binding proteins to bio-inspired antifreeze materials.Soft matter · 2017Review
- Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant.Marine drugs · 2017Review
- Investigation of changes in structure and thermodynamic of spruce budworm antifreeze protein under subfreezing temperature.Scientific reports · 2017Article
- Janus effect of antifreeze proteins on ice nucleation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Microfluidic Cold-Finger Device for the Investigation of Ice-Binding Proteins.Biophysical journal · 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
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ice-binding proteins that aid the survival of freeze-avoiding, cold-adapted organisms by inhibiting the growth of endogenous ice crystals are called antifreeze proteins (AFPs). The binding of AFPs to ice causes a separation between the melting point and the freezing point of the ice crystal (thermal hysteresis, TH). TH produced by hyperactive AFPs is an order of magnitude higher than that produced by a typical fish AFP. The basis for this difference in activity remains unclear. Here, we have compared the time dependence of TH activity for both hyperactive and moderately active AFPs using a custom-made nanolitre osmometer and a novel microfluidics system. We found that the TH activities of hyperactive AFPs were time-dependent, and that the TH activity of a moderate AFP was almost insensitive to time. Fluorescence microscopy measurement revealed that despite their higher TH activity, hyperactive AFPs from two insects (moth and beetle) took far longer to accumulate on the ice surface than did a moderately active fish AFP. An ice-binding protein from a bacterium that functions as an ice adhesin rather than as an antifreeze had intermediate TH properties. Nevertheless, the accumulation of this ice adhesion protein and the two hyperactive AFPs on the basal plane of ice is distinct and extensive, but not detectable for moderately active AFPs. Basal ice plane binding is the distinguishing feature of antifreeze hyperactivity, which is not strictly needed in fish that require only approximately 1°C of TH. Here, we found a correlation between the accumulation kinetics of the hyperactive AFP at the basal plane and the time sensitivity of the measured TH.
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