Antifreeze protein - Knowledge (XXG)

1115:) and Notothenioids is supported by the findings of different spacer sequences and different organization of introns and exons as well as unmatching AFGP tripeptide sequences, which emerged from duplications of short ancestral sequences which were differently permuted (for the same tripeptide) by each group. These groups diverged approximately 7-15 million years ago. Shortly after (5-15 mya), the AFGP gene evolved from an ancestral pancreatic trypsinogen gene in Notothenioids. AFGP and trypsinogen genes split via a sequence divergence - an adaptation which occurred alongside the cooling and eventual freezing of the Antarctic Ocean. The evolution of the AFGP gene in Northern cod occurred more recently (~3.2 mya) and emerged from a noncoding sequence via tandem duplications in a Thr-Ala-Ala unit. Antarctic notothenioid fish and artic cod, Boreogadus saida, are part of two distinct orders and have very similar antifreeze glycoproteins. Although the two fish orders have similar antifreeze proteins, cod species contain arginine in AFG, while Antarctic notothenioid do not. The role of arginine as an enhancer has been investigated in Dendroides canadensis antifreeze protein (DAFP-1) by observing the effect of a chemical modification using 1-2 cyclohexanedione. Previous research has found various enhancers of this bettles' antifreeze protein including a thaumatin-like protein and polycarboxylates. Modifications of DAFP-1 with the arginine specific reagent resulted in the partial and complete loss of thermal hysteresis in DAFP-1, indicating that arginine plays a crucial role in enhancing its ability. Different enhancer molecules of DAFP-1 have distinct thermal hysteresis activity. Amornwittawat et al. 2008 found that the number of carboxylate groups in a molecules influence the enhancing ability of DAFP-1. Optimum activity in TH is correlated with high concentration of enhancer molecules. Li et al. 1998 investigated the effects of pH and solute on thermal hysteresis in Antifreeze proteins from Dendrioides canadensis. TH activity of DAFP-4 was not affected by pH unless the there was a low solute concentration (pH 1) in which TH decreased. The effect of five solutes; succinate, citrate, malate, malonate, and acetate, on TH activity was reported. Among the five solutes, citrate was shown to have the greatest enhancing effect. 944:, but the disulfide-braced beta-solenoid is formed from shorter 10 amino-acids repeats, and instead of threonine, the ice-binding surface consists of a single row of tyrosine residues. Springtails (Collembola) are not insects, but like insects, they are arthropods with six legs. A species found in Canada, which is often called a "snow flea", produces hyperactive AFPs. Although they are also repetitive and have a flat ice-binding surface, the similarity ends there. Around 50% of the residues are glycine (Gly), with repeats of Gly-Gly- X or Gly-X-X, where X is any amino acid. Each 3-amino-acid repeat forms one turn of a polyproline type II helix. The helices then fold together, to form a bundle that is two helices thick, with an ice-binding face dominated by small hydrophobic residues like alanine, rather than threonine. Other insects, such as an Alaskan beetle, produce hyperactive antifreezes that are even less similar, as they are polymers of sugars ( 1190:

studies on type I AFP, ice and AFP were initially thought to interact through hydrogen bonding (Raymond and DeVries, 1977). However, when parts of the protein thought to facilitate this hydrogen bonding were mutated, the hypothesized decrease in antifreeze activity was not observed. Recent data suggest hydrophobic interactions could be the main contributor. It is difficult to discern the exact mechanism of binding because of the complex water-ice interface. Currently, attempts to uncover the precise mechanism are being made through use of

2054: 1161:). Ice antifreeze proteins have been reported in diatom species to help decrease the freezing point of organism's proteins. Bayer-Giraldi et al. 2010 found 30 species from distinct taxa with homologues of ice antifreeze proteins. The diversity is consistent with previous research that has observed the presence of these genes in crustaceans, insects, bacteria, and fungi. Horizontal gene transfer is responsible for the presence of ice antifreeze proteins in two sea diatom species, F. cylindrus and F. curta. 1291:

to isolate the antifreeze protein through his investigation of Antarctic fish. These proteins were later called antifreeze glycoproteins (AFGPs) or antifreeze glycopeptides to distinguish them from newly discovered nonglycoprotein biological antifreeze agents (AFPs). DeVries worked with Robert Feeney (1970) to characterize the chemical and physical properties of antifreeze proteins. In 1992, Griffith

842:. They exhibit similar overall hydrophobicity at ice binding surfaces to type I AFPs. They are approximately 6kD in size. Type III AFPs likely evolved from a sialic acid synthase (SAS) gene present in Antarctic eelpout. Through a gene duplication event, this gene—which has been shown to exhibit some ice-binding activity of its own—evolved into an effective AFP gene by loss of the N-terminal part. 734:: These species are able to survive body fluid freezing. Some freeze tolerant species are thought to use AFPs as cryoprotectants to prevent the damage of freezing, but not freezing altogether. The exact mechanism is still unknown. However, it is thought AFPs may inhibit recrystallization and stabilize cell membranes to prevent damage by ice. They may work in conjunction with ice 191: 44: 835:. If the AFP gene were present in the most recent common ancestor of these lineages, it is peculiar that the gene is scattered throughout those lineages, present in some orders and absent in others. It has been suggested that lateral gene transfer could be attributed to this discrepancy, such that the smelt acquired the type II AFP gene from the herring. 931:) have longer repeats without internal disulfide bonds that form a compressed beta-solenoid (beta sandwich) with four rows of threonine residus, and this AFP is structurally similar to that modelled for the non-homologous AFP from the pale beauty moth. In contrast, the AFP from the spruce budworm moth is a solenoid that superficially resembles the 759: 706:. Organisms differ in their values of thermal hysteresis. The maximum level of thermal hysteresis shown by fish AFP is approximately −3.5 °C (Sheikh Mahatabuddin et al., SciRep)(29.3 °F). In contrast, aquatic organisms are exposed only to −1 to −2 °C below freezing. During the extreme winter months, the 1290:

In the 1950s, Norwegian scientist Scholander set out to explain how Arctic fish can survive in water colder than the freezing point of their blood. His experiments led him to believe there was “antifreeze” in the blood of Arctic fish. Then in the late 1960s, animal biologist Arthur DeVries was able

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Type I-hyp AFP (where hyp stands for hyperactive) are found in several righteye flounders. It is approximately 32 kD (two 17 kD dimeric molecules). The protein was isolated from the blood plasma of winter flounder. It is considerably better at depressing freezing temperature than most fish AFPs. The

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AFPs create a difference between the melting point and freezing point (busting temperature of AFP bound ice crystal) known as thermal hysteresis. The addition of AFPs at the interface between solid ice and liquid water inhibits the thermodynamically favored growth of the ice crystal. Ice growth is

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beetles are homologous and each 12–13 amino-acid repeat is stabilized by an internal disulfide bond. Isoforms have between 6 and 10 of these repeats that form a coil, or beta-solenoid. One side of the solenoid has a flat ice-binding surface that consists of a double row of threonine residues. Other

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Normally, ice crystals grown in solution only exhibit the basal (0001) and prism faces (1010), and appear as round and flat discs. However, it appears the presence of AFPs exposes other faces. It now appears the ice surface 2021 is the preferred binding surface, at least for AFP type I. Through

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occurring 1–2 million years ago in the Northern hemisphere and 10-30 million years ago in Antarctica. Data collected from deep sea ocean drilling has revealed that the development of the Antarctic Circumpolar Current was formed over 30 million years ago. The cooling of Antarctic imposed from this

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In fishes, horizontal gene transfer is responsible for the presence of Type II AFP proteins in some groups without a recently shared phylogeny. In Herring and smelt, up to 98% of introns for this gene are shared; the method of transfer is assumed to occur during mating via sperm cells exposed to

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beetles, spruce budworm and pale beauty moths, and midges (same order as flies). Insect AFPs share certain similarities, with most having higher activity (i.e. greater thermal hysteresis value, termed hyperactive) and a repetitive structure with a flat ice-binding surface. Those from the closely

1376:(GMOs) who believe that antifreeze proteins may cause inflammation. Intake of AFPs in diet is likely substantial in most northerly and temperate regions already. Given the known historic consumption of AFPs, it is safe to conclude their functional properties do not impart any toxicologic or 713:

The rate of cooling can influence the thermal hysteresis value of AFPs. Rapid cooling can substantially decrease the nonequilibrium freezing point, and hence the thermal hysteresis value. Consequently, organisms cannot necessarily adapt to their subzero environment if the temperature drops

800:. It is the best documented AFP because it was the first to have its three-dimensional structure determined. Type I AFP consists of a single, long, amphipathic alpha helix, about 3.3-4.5 kD in size. There are three faces to the 3D structure: the hydrophobic, hydrophilic, and Thr-Asx face. 1433:

A 2010 study demonstrated the stability of superheated water ice crystals in an AFP solution, showing that while the proteins can inhibit freezing, they can also inhibit melting. In 2021, EPFL and Warwick scientists have found an artificial imitation of antifreeze proteins.

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Light Double Churned ice cream bars. In ice cream, AFPs allow the production of very creamy, dense, reduced fat ice cream with fewer additives. They control ice crystal growth brought on by thawing on the loading dock or kitchen table, which reduces texture quality.

948:) rather than polymers of amino acids (proteins). Taken together, this suggests that most of the AFPs and antifreezes arose after the lineages that gave rise to these various insects diverged. The similarities they do share are the result of convergent evolution. 1295:

documented their discovery of AFP in winter rye leaves. Around the same time, Urrutia, Duman and Knight (1992) documented thermal hysteresis protein in angiosperms. The next year, Duman and Olsen noted AFPs had also been discovered in over 23 species of

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Antifreeze glycoprotein activity has been observed across several ray-finned species including eelpouts, sculpins, and cod species. Fish species that possess the antifreeze glycoprotein express different levels of protein activity. Polar cod

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current caused a mass extinction of teleost species that were unable to withstand freezing temperatures. Notothenioids species with the antifreeze gylcoprotein were able to survive the glaciation event and diversify into new niches.

851:) are found in longhorn sculpins. They are alpha helical proteins rich in glutamate and glutamine. This protein is approximately 12KDa in size and consists of a 4-helix bundle. Its only posttranslational modification is a 1308:

Recent attempts have been made to relabel antifreeze proteins as ice structuring proteins to more accurately represent their function and to dispose of any assumed negative relation between AFPs and automotive antifreeze,

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IBP) is enough for the total inhibition of ice re-crystallization in –7.4 °C temperature. This ice-recrystallization inhibition ability helps bacteria to tolerate ice rather than preventing the formation of ice.

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Haymet AD, Ward LG, Harding MM (1999). "Winter Flounder 'anti-freeze' proteins: Synthesis and ice growth inhibition of analogues that probe the relative importance of hydrophobic and hydrogen bonding interactions".

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of ice that would otherwise be fatal. There is also increasing evidence that AFPs interact with mammalian cell membranes to protect them from cold damage. This work suggests the involvement of AFPs in cold

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are produced using this technology. The process does not impact the product; it merely makes production more efficient and prevents the death of fish that would otherwise be killed to extract the protein.

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protein, with a similar ice-binding surface, but it has a triangular cross-section, with longer repeats that lack the internal disulfide bonds. The AFP from midges is structurally similar to those from

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Do H, Kim SJ, Kim HJ, Lee JH (April 2014). "Structure-based characterization and antifreeze properties of a hyperactive ice-binding protein from the Antarctic bacterium Flavobacterium frigoris PS1".

728:: These species are able to prevent their body fluids from freezing altogether. Generally, the AFP function may be overcome at extremely cold temperatures, leading to rapid ice growth and death. 1118:

This is an example of a proto-ORF model, a rare occurrence where new genes pre exist as a formed open reading frame before the existence of the regulatory element needed to activate them.

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One recent, successful business endeavor has been the introduction of AFPs into ice cream and yogurt products. This ingredient, labelled ice-structuring protein, has been approved by the

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manner. This phenomenon allows them to act as an antifreeze at concentrations 1/300th to 1/500th of those of other dissolved solutes. Their low concentration minimizes their effect on

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Mangiagalli M, Bar-Dolev M, Tedesco P, Natalello A, Kaleda A, Brocca S, et al. (January 2017). "Cryo-protective effect of an ice-binding protein derived from Antarctic bacteria".

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The classification of AFPs became more complicated when antifreeze proteins from plants were discovered. Plant AFPs are rather different from the other AFPs in the following aspects:

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yeast to produce antifreeze proteins from fish for use in ice cream production. They are labeled "ISP" or ice structuring protein on the label, instead of AFP or antifreeze protein.

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foreign DNA. The direction of transfer is known to be from herring to smelt as herring have 8 times the copies of AFP gene as smelt (1) and the segments of the gene in smelt house

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play a key role in polar sea ice communities, dominating the assemblages of both platelet layer and within pack ice. AFPs are widespread in these species, and the presence of AFP

3688:"Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis: Antifreeze protein from ascomycetous fungus" 784:. They are 2.6-3.3 kD. AFGPs evolved separately in notothenioids and northern cod. In notothenioids, the AFGP gene arose from an ancestral trypsinogen-like serine protease gene. 1216:, the antifreeze mechanism of the type-I AFP molecule was shown to be due to the binding to an ice nucleation structure in a zipper-like fashion through hydrogen bonding of the 2625:

Bayer-Giraldi M, Uhlig C, John U, Mock T, Valentin K (April 2010). "Antifreeze proteins in polar sea ice diatoms: diversity and gene expression in the genus Fragilariopsis".

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Kelley JL, Aagaard JE, MacCoss MJ, Swanson WJ (August 2010). "Functional diversification and evolution of antifreeze proteins in the antarctic fish Lycodichthys dearborni".

690:. The unusual properties of AFPs are attributed to their selective affinity for specific crystalline ice forms and the resulting blockade of the ice-nucleation process. 1133:

Although ice is uniformly composed of water molecules, it has many different surfaces exposed for binding. Different types of AFPs may interact with different surfaces.

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Duman JG, de Vries AL (1976). "Isolation, characterization, and physical properties of protein antifreezes from the winter flounder, Pseudopleuronectes americanus".

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Numerous fields would be able to benefit from the protection of tissue damage by freezing. Businesses are currently investigating the use of these proteins in:

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residue (or any other polar amino acid residue whose side-chain can form a hydrogen bond with water) in an 11-amino-acid period along the sequence concerned, and

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of ice, inhibiting thermodynamically-favored ice growth. The presence of a flat, rigid surface in some AFPs seems to facilitate its interaction with ice via

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Graham LA, Marshall CB, Lin FH, Campbell RL, Davies PL (February 2008). "Hyperactive antifreeze protein from fish contains multiple ice-binding sites".

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The above mechanism can be used to elucidate the structure-function relationship of other antifreeze proteins with the following two common features:

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Ewart KV, Rubinsky B, Fletcher GL (May 1992). "Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins".

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Hoshino T, Kiriaki M, Ohgiya S, Fujiwara M, Kondo H, Nishimiya Y, Yumoto I, Tsuda S (December 2003). "Antifreeze proteins from snow mold fungi".

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Lin FH, Davies PL, Graham LA (May 2011). "The Thr- and Ala-rich hyperactive antifreeze protein from inchworm folds as a flat silk-like β-helix".

2868:"Hyperactive antifreeze protein from an Antarctic sea ice bacterium Colwellia sp. has a compound ice-binding site without repetitive sequences" 2256:

Liou YC, Tocilj A, Davies PL, Jia Z (July 2000). "Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein".

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Scotter AJ, Marshall CB, Graham LA, Gilbert JA, Garnham CP, Davies PL (October 2006). "The basis for hyperactivity of antifreeze proteins".

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Wang, Sen; Amornwittawat, Natapol; Juwita, Vonny; Kao, Yu; Duman, John G.; Pascal, Tod A.; Goddard, William A.; Wen, Xin (2009-10-13).

831:. Type II AFPs likely evolved from calcium dependent (c-type) lectins. Sea ravens, smelt, and herring are quite divergent lineages of 4309: 3621: 1450:

Daley ME, Spyracopoulos L, Jia Z, Davies PL, Sykes BD (April 2002). "Structure and dynamics of a beta-helical antifreeze protein".

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direction in ice lattice, subsequently stopping or retarding the growth of ice pyramidal planes so as to depress the freeze point.

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IBP produces also thermal hysteresis gap, but this ability is not as efficient as the ice-recrystallization inhibition ability.

2395:"Intermediate activity of midge antifreeze protein is due to a tyrosine-rich ice-binding site and atypical ice plane affinity" 1030:

that form a flat ice-binding surface. Unlike the other AFPs, there is not a singular sequence motif for the ice-binding site.

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Xiao, Nan; Suzuki, Keita; Nishimiya, Yoshiyuki; Kondo, Hidemasa; Miura, Ai; Tsuda, Sakae; Hoshino, Tamotsu (January 2010).

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Their physiological function is likely in inhibiting the recrystallization of ice rather than in preventing ice formation.

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Barker PF, Thomas E (June 2004). "Origin, signature and palaeoclimatic influence of the Antarctic Circumpolar Current".

2553:"A nonprotein thermal hysteresis-producing xylomannan antifreeze in the freeze-tolerant Alaskan beetle Upis ceramboides" 2501:"X-ray structure of snow flea antifreeze protein determined by racemic crystallization of synthetic protein enantiomers" 1366: 1099:

The remarkable diversity and distribution of AFPs suggest the different types evolved recently in response to sea level

3225:"A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins" 983:

belong to an AFP family which is represented in different taxa and can be found in other organisms related to sea ice (

1927:"Structure of an antifreeze polypeptide from the sea raven. Disulfide bonds and similarity to lectin-binding proteins" 4500:

Sicheri F, Yang DS (June 1995). "Ice-binding structure and mechanism of an antifreeze protein from winter flounder".

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Crevel RW, Fedyk JK, Spurgeon MJ (July 2002). "Antifreeze proteins: characteristics, occurrence and human exposure".

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of amino acids, when each folds into a functioning protein they may share similarities in their three-dimensional or

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Raymond JA, Christner BC, Schuster SC (September 2008). "A bacterial ice-binding protein from the Vostok ice core".

2125:"Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis" 4271: 3600:

Feeney RE, Yeh Y (1978-01-01). Anfinsen CB, Edsall JT, Richards FM (eds.). "Antifreeze proteins from fish bloods".

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Kiko R (April 2010). "Acquisition of freeze protection in a sea-ice crustacean through horizontal gene transfer?".

3853:"Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm" 1058: 3168:"Arginine, a Key Residue for the Enhancing Ability of an Antifreeze Protein of the Beetle Dendroides canadensis" 4360:"Ice recrystallization inhibition in ice cream as affected by ice structuring proteins from winter wheat grass" 197: 4290: 1129:

There are two reasons why many types of AFPs are able to carry out the same function despite their diversity:

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Griffith M, Yaish MW (August 2004). "Antifreeze proteins in overwintering plants: a tale of two activities".

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Raymond JA, Fritsen C, Shen K (August 2007). "An ice-binding protein from an Antarctic sea ice bacterium".

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Clarke CJ, Buckley SL, Lindner N (2002). "Ice structuring proteins - a new name for antifreeze proteins".

3647:"Cold survival in freeze-intolerant insects: The structure and function of β-helical antifreeze proteins" 3509:

Raymond JA, Lin Y, DeVries AL (July 1975). "Glycoprotein and protein antifreezes in two Alaskan fishes".

4452: 1369:. The proteins are isolated from fish and replicated, on a larger scale, in genetically modified yeast. 1019: 1007: 3687: 1487:"A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights" 1313:. These two things are completely separate entities, and show loose similarity only in their function. 598: 300: 153: 4019:

Chou KC (January 1992). "Energy-optimized structure of antifreeze protein and its binding mechanism".

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published the discovery of a molecule in an Alaskan beetle that behaves like AFPs, but is composed of

4616: 4509: 4412: 4063: 3921: 3864: 3805: 3746: 3553: 3463: 3117: 3017: 2564: 2265: 2076: 2014: 1771: 1354: 1123: 1108: 747: 494: 440: 374: 257: 110: 4107:"Chemical and physical properties of freezing point-depressing glycoproteins from Antarctic fishes" 2499:

Pentelute BL, Gates ZP, Tereshko V, Dashnau JL, Vanderkooi JM, Kossiakoff AA, Kent SB (July 2008).

1191: 1178: 703: 1760:"Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish" 657:

that permit their survival in temperatures below the freezing point of water. AFPs bind to small

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has obtained UK, US, EU, Mexico, China, Philippines, Australia and New Zealand approval to use a

1199: 1195: 1141: 3452:"Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod" 3106:"Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod" 2774: 1057:

IBP helps to protect both purified proteins and whole bacterial cells in freezing temperatures.

1300:, including ones eaten by humans. They reported their presence in fungi and bacteria as well. 1040:

and psychrophilic bacteria has an efficient ice re-crystallization inhibition ability. 1 μM of

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Raymond JA, Janech MG (April 2009). "Ice-binding proteins from enoki and shiitake mushrooms".

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Increasing freeze tolerance of crop plants and extending the harvest season in cooler climates

1137: 1002: 797: 682:, AFPs do not lower freezing point in proportion to concentration. Rather, they work in a non 589: 291: 144: 4525: 4517: 4480: 4420: 4371: 4194: 4183:"Thermal hysteresis protein activity in bacteria, fungi and phylogenetically diverse plants" 4155: 4118: 4071: 4028: 3978: 3937: 3929: 3880: 3872: 3823: 3813: 3764: 3754: 3699: 3658: 3609: 3561: 3518: 3481: 3471: 3406: 3354: 3306: 3290: 3236: 3195: 3179: 3135: 3125: 3067: 3025: 2972: 2964: 2924: 2879: 2840: 2813: 2786: 2739: 2704: 2669: 2634: 2582: 2572: 2520: 2512: 2454: 2406: 2367: 2330: 2320: 2273: 2230: 2188: 2180: 2136: 2084: 2032: 2022: 1975: 1938: 1899: 1864: 1829: 1789: 1779: 1727: 1685: 1643: 1635: 1589: 1540: 1498: 1459: 1404: 1067: 1013: 793: 687: 50: 1126:

which are otherwise characteristic of and common in herring but not found in other fishes.

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Several structures for sea ice AFPs have been solved. This family of proteins fold into a

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Graham LA, Davies PL (October 2005). "Glycine-rich antifreeze proteins from snow fleas".

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DeVries AL, Wohlschlag DE (March 1969). "Freezing resistance in some Antarctic fishes".

3967:"Valine substituted winter flounder 'antifreeze': preservation of ice growth hysteresis" 3925: 3910:"Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes" 3868: 3809: 3750: 3557: 3467: 3121: 3021: 2568: 2309:"Crystal structure of an insect antifreeze protein and its implications for ice binding" 2269: 2080: 2018: 1775: 3942: 3909: 3885: 3852: 3311: 3278: 3200: 3167: 2587: 2552: 2525: 2500: 2335: 2308: 2193: 2168: 2037: 2002: 1648: 1623: 1217: 828: 707: 4123: 4106: 3983: 3966: 3933: 3876: 3828: 3793: 3769: 3734: 3613: 2141: 2124: 1979: 1943: 1926: 1731: 1227: 4605: 4590: 4249: 4159: 4032: 3703: 3663: 3646: 3486: 3451: 3436: 3140: 3105: 2673: 2638: 2482:"New Antifreeze Protein Found In Fleas May Allow Longer Storage Of Transplant Organs" 1833: 1794: 1759: 1689: 1593: 852: 770: 486: 432: 415: 366: 249: 102: 4091: 4000: 3581: 3343:"Enhancement of insect antifreeze protein activity by solutes of low molecular mass" 3029: 2994: 2716: 2604: 2474: 2428: 2307:

Hakim A, Nguyen JB, Basu K, Zhu DF, Thakral D, Davies PL, et al. (April 2013).

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Duman JG (2001). "Antifreeze and ice nucleator proteins in terrestrial arthropods".

543: 225: 78: 3719: 3087: 2901: 2844: 2293: 1868: 1544: 1423: 889: 820: 777: 658: 638: 577: 279: 132: 4547: 4075: 2775:"Antifreeze activities of various fungi and Stramenopila isolated from Antarctica" 2759: 2234: 804:

ability is partially derived from its many repeats of the Type I ice-binding site.

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Urrutia ME, Duman JG, Knight CA (May 1992). "Plant thermal hysteresis proteins".

3565: 3294: 2027: 1624:"Theoretical study of interaction of winter flounder antifreeze protein with ice" 1485:

Leinala EK, Davies PL, Doucet D, Tyshenko MG, Walker VK, Jia Z (September 2002).

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kinetically inhibited by the AFPs covering the water-accessible surfaces of ice.

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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

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Yang DS, Hon WC, Bubanko S, Xue Y, Seetharaman J, Hew CL, Sicheri F (May 1998).

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Fletcher GL, Hew CL, Davies PL (2001). "Antifreeze proteins of teleost fishes".

1548: 1335: 1297: 1174: 1091:. Also, all the ice-binding polar residues are at the same site of the protein. 1088: 683: 4425: 4400: 3798: