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Antifreeze protein
Non-colligative properties
In contrast to the widely used automotive antifreeze, ethylene glycol, it is not freezing AFPs lower relative to the concentration. Rather, they work in a non-colligative manner. This allows them as antifreeze in concentrations of 300 and 500 times smaller than other dissolved solutes act. This minimizes the effect on the osmotic pressure. The AFPs are unusual skills, their ability to bind to certain surfaces of the Attributed to ice crystals.
Thermal hysteresis
AFP is a difference between the melting point and freezing point known as thermal hysteresis. The addition of AFPs at the interface between solid ice and liquid water inhibits the thermodynamically favorable for the growth of ice crystals. Ice growth is kinetically inhibited by the AFPs for the water-accessible Surfaces of ice.
Thermal hysteresis is easily measured in the laboratory with a nanoliter osmometer. Different organisms have different values of the thermal hysteresis. The maximum Amount of thermal hysteresis of AFP in fish around -1.5 C (2.7 F). However, insect antifreeze proteins 1030 times more active than any known fish protein. This is probably because insects encounter lower temperatures on land as the 1C or 2C, that fish face freezing waters. During the extreme winter temperatures spruce budworm can battle withstand near freezing and 30C, although the Alaskan beetle Upis ceramboides can survive in a temperature range of 60C by using an antifreeze molecule, that is not composed of proteins.
The cooling rate can affect the thermal hysteresis value of AFPs. Rapid cooling significantly reduce non-equilibrium freezing Point and therefore the thermal hysteresis. This means that organisms are not able to adapt their environment subzero when the temperature drops suddenly.
Freeze tolerance Freeze avoidance
Species with AFPs can classified as follows:
Freeze avoiding: These species are capable of their body fluids from freezing entirely to prevent. In general, the AFP-function can be overcome by extremely cold temperatures, leading to a rapid growth of ice and death.
Freeze tolerant: These species are Able to survive body fluid freezing. Some freeze-tolerant species are probably using AFP as a cryoprotectant to prevent freezing damage, but not quite freezing. The exact mechanism is still unknown. However, it is thought that AFPs may inhibit recrystallization and stabilize the cell membranes to damage to prevent ice. They can be combined with protein ice nucleators (PINs) are working to speed the spread ice control following freezing.
Diversity
There are many known types of non-homologous AFP.
Fish AFPs
Figure 1 The three faces of type I AFP
Antifreeze glycoproteins, or AFGPs in Antarctica and found in the northern cod notothenioids. They are 2.6 to 3.3 kD.
Type I AFPs in winter flounder and shorthorn sculpin displayed. They are the best documented AFP, because it was the first to have determined the 3D structure. Type I AFPs consist of a single, long, amphipathic alpha-helix. They are about 3.3 to 4.5 kD in size. There are three faces the 3D structure: the hydrophobic, hydrophilic, and Thr-Asx face.
Type I AFP-Hyp (where Hyp stands for hyperactive) are found in several righteye flounders. It is about 32 kD (two 17 kD dimeric molecule). The protein was isolated from the blood plasma of winter flounder. It is much better depressing freezing temperature than most fish AFPs.
Type II AFPs are found cormorants, smelt and herring. They are cysteine-rich globular proteins with five disulfide bridges.
Type III AFPs are found in the Antarctic eelpout. You have similar overall hydrophobicity in ice binding surfaces of type I AFPs. They are about 6kD large.
Type IV AFPs are found in Longhorn sculpins. They are alpha helical protein rich in glutamate and glutamine. This protein is about 12KDa and consists of a 4-helix bundle. His only post-translational modification is a pyroglutamate Residue, a cyclized glutamine residue at its N-terminal. Scientists at the University of Guelph in Canada, currently the role of this residue pyroglutame check the antifreeze Activity of type IV AFP sculpin from Longhorn.
Insect AFPs
Cartoon representation of the molecular structure of an insect cysteine-rich antifreeze protein.
Type V AFPs are hyperactive (ie, higher thermal hysteresis value) found in insect AFPs.
Tenebrio AFPs dendroides and are both found in different insect families. They are very similar each other. These AFPs consist of different number of 12 – or 13-mer repeats of about 8.3 to 12.5 kD. During the entire length of the amino acid, at least one in six is a cysteine residue. They are also hyperactive.
Plant AFPS
The classification of AFP was further complicated when antifreeze proteins have been discovered from plants. Plant AFPs are quite different from the other AFPs in the following aspects:
They have much less thermal hysteresis activity compared to other AFPs.
The physiological Function is probably in the inhibition of recrystallization of ice instead of in the prevention of ice formation.
Most of them are pathogenesis-related proteins, sometimes retaining antifungal properties developed.
See also dehydrin
Evolution
The remarkable diversity and distribution of AFPs suggests that the different species from recently arisen before in response to sea level glaciation occurring 1-2 million years in the northern hemisphere and 10-30 million years ago in Antarctica. This independent Development of similar adaptations is called convergent evolution. There are two reasons why many types of AFPs are able to bear the same function in spite of their diversity: 1. Although ice is uniformly composed of oxygen and hydrogen, it has exposed many different surfaces for binding. Different types of AFPs can be different interacting surfaces. 2. Although the five types of AFPs differ in their primary sequence of amino acids, if at any folds into a functional protein they share similarities in their 3D or tertiary structure, the same interactions facilitated the ice.
Mechanisms
AFPs are thought to the growth adsorptionnhibition a mechanism inhibiting. They adsorb on non-basal planes of ice, ice-inhibiting thermodynamically favored growth. The presence of a flat, solid surface in AFPs seems its interaction with ice of Van der Waals force to facilitate surface complementarity.
The binding to ice
Normally, ice crystals only grown in the solution shows the basal (0001) and prism faces (1010) and appear as round and flat discs. It seems, however, the presence of AFPs makes more faces. It appears now that the ice surface 2021 is preferred binding surface, at least for AFP type I. Investigations on Type I AFP, was initially thought that ice and AFP via hydrogen bonds (Raymond and DeVries, 1977) interacts. However, if parts of the protein, thought to facilitate the hydrogen bonds were mutated, the decline suspected anti-freeze in activity was observed. Recent data show that hydrophobic interactions could be the most important factor. It is difficult to determine the exact mechanism the binding seen for the complex water-ice interface. Currently trying to determine the exact mechanism by the use of molecular modeling programs (molecular dynamics or Monte-Carlo method) . Uncover
History
In the 1950s, Canadian researchers set out to explain Scholander, to Arctic fish can in the water colder than the freezing point of their Blood to survive. His experiments led him to believe it was ntifreeze in the blood of Arctic fish. Then in the late 1960s, animal biologist Arthur DeVries of the situation, to isolate the antifreeze protein by its investigation of the Antarctic fish. AFGPs were the first to be discovered AFPs. By the time they were called "glycoproteins as biological Antifreeze. These proteins were later antifreeze glycoproteins (AFGPs) or antifreeze glycopeptides called them different from newly discovered non-glycoprotein biological anti-freeze (AFP). DeVries worked with Robert Feeney (1970) on the chemical and physical properties of antifreeze proteins characterized. In 1992, Griffith et al. documented their discovery of the AFP in winter rye leaves. Around the same time, Urrutia, Duman and Knight (1992) documented thermal hysteresis protein in angiosperms. The next year, presented Duman and Olsen AFPs had in over 23 species of flowering plants that have been discovered among them also those eaten by people. As well, she reported their presence in fungi and bacteria.
Name Change
Recent attempts have been made to antifreeze proteins, such as ice structuring proteins in order Relabel accurate representation of your function and assumed to dispose of any negative relationship between AFPs and automotive antifreeze, ethylene glycol. These two things are completely separate entities, and only a loose resemblance to show their function.
Commercial applications
Commercially, it seems to be countless applications for anti-freeze proteins. Many fields of Would be able to benefit from the protection of tissue injury by freezing. The companies are currently using these proteins in:
Increase freeze tolerance of crops and extending the harvest season in cooler climates
Improving farm fish production in cooler climates
Extending shelf life of frozen food
Improvement of cryosurgery
Improve the preservation of tissues for transplantation or transfusion in medicine
Therapy for hypothermia
Current News
A more recent effort, successful businessmen, the introduction of AFPs to ice was and yogurt products. This drug, called ice-structuring Protein, was approved by the Food and Drug Administration. The proteins are isolated from fish and reproduced on a larger scale in yeast.
The fear is changed from anti-GM (GM) organizations, arguing antifreeze proteins can cause inflammation. However, as I said, ISPs have been approved for human consumption diligently testing. Intake of AFPs in the diet is likely to be substantially in the most northern and temperate regions already. Given the known historical use of AFPs, it is safe to conclude, do not give their functional properties, toxicological or allergenic effects in humans.
How good is the transgenic production process, the ISP used extensively in society already. This is how mass amounts of insulin are made to people to deal with Type I diabetes each year. The method has no effect on the product, it just provides more efficient production and prevented the deaths of many fish that would otherwise be killed for the production of such protein.
Unilever AFPs currently includes in some of its products, including some ice lollies and a new line of Breyer Light Double Churned ice cream bars. In ice, AFPs allow the production of very creamy, dense, reduced-fat ice creams with fewer additives. They control ice crystal growth caused by thawing on the loading dock or kitchen table, which drastically reduces texture quality.
published in November 2009, Proceedings of the National Academy of Sciences the discovery of a molecule in an Alaskan beetle, which behaves as AFPs, but is composed of saccharides and fatty acids
References
^ Abc J. Madura. (2001). Digested proteins: Projects in Scientific Computing
^ Abcdef GL Fletcher, CL Hew and PL Davies. (2001). Teleost fish antifreeze proteins. Annu. Rev. Physiol. 63 35 990
^ Abcd A. Jorov, BS and DS Zhorov Yang. (2004). Theoretical study of interaction of winter flounder antifreeze protein with ice. Protein Science. 13, 1524-1537
^ Walters KR Jr, Serianni AS, Sformo T, Barnes BM, Duman JG (2009). "A non-protein thermal hysteresis producing antifreeze xylomannan in the freeze-tolerant beetles Alaskan Upis ceramboides "(HTML). PNAS Epub ahead of print. PMID 19,934,038th
Abc ^ JG Duman. (2001). Antifreeze and ice nucleator proteins in terrestrial arthropods. Annu. Rev. Physiol. 63, 32757th
^ Abcd RWR Crevel, JK Fedyk and MJ Spurgeon. (2002). Antifreeze proteins: properties, occurrence and human exposure (Review). Food and Chemical Toxicology 20, 899-903.
^ From J. Duman and AL DeVries. (1976). Isolation, characterization and physical properties of antifreeze protein from winter flounder Pseudopleunectus Americanus. Comp. Biochem. Physiol. B54, 375,380th
^ Scotter, AJ, et al. (2006). "The basis for hyperactivity of antifreeze proteins." Cryobiology 53 (2): 229,239th doi: 10.1016/j.cryobiol.2006.06.006. PMID 16,887,111th
^ N. C. Ng and Hew (1992). Structure of the polypeptide from the sea raven antifreeze: disulfide bonds and similarity to lectin-binding proteins. J. Biol. Chem 267, 16069-16075.
^ Abc G. Deng, DW Andrews and RA Laursen. (1997). Amino acid sequence of a new type of Antifreeze protein from the longhorn sculpin octodecimspinosis Myoxocephalus. FEBS Lett. 402:1, 17-20.
^ Graham, Laurie A., et al. (1997). "Hyperactive antifreeze protein of beetles, "Nature 388 (6644). 727,728th. doi: 10.1038/41908 PMID http://www.nature.com/nature/journal/v388/n6644/abs/388727a0.html 9285581st.
^ M. Griffith et al. (1992). Antifreeze protein produced endogenously in winter rye leaves. Plant Physiology 100:2, 593-596.
^ Abc M. Griffith and M. Yaish. (2004). Antifreeze proteins plants in the winter: A Tale of Two activities. Trends in Plant Science 09:08, 399-405.
^ Convergent evolution of antifreeze glycoproteins in Arctic and Antarctic notothenioid Cod fish
^ Raymond, J., DeVries, AL (1977). "Adsorption inhibition as a mechanism of freezing resistance in polar fishes. PNAS 74 (6): 25,892,593th doi: 10.1073/pnas.74.6.2589. http://www.pnas.org/content/74/6/2589.abstract.
^ Raymond, J., et al. (1989). "The inhibition of growth of nonbasal aircraft in the ice of fish antifreeze "PNAS 86 (3). 881,885th doi:. 10.1073/pnas.86.3.881 PMID 2,915,983th PMC 286582nd http://www.pnas.org/content/86/3/881.abstract .
^ Yang, DS, et al. (1998). "Identification of the ice-binding surface on a type III antifreeze protein with a" flatness function "algorithm". Biophysical Journal 74 (5): 21,422,151th doi: 10.1016/S0006-3495 (98) 77923-8. PMID 9591641st
^ C night, C. Cheng and A. DeVries. (1991). Adsorption of alpha-helical peptides Anti-freeze ice on certain aircraft. Biophys. J. 59, 409-418.
^ A. Haymett, L. Ward and M. Harding. (1998). Valine replaced Winter flounder "antifreeze": Preservation of ice growth hysteresis. FEBS Lett. 430, 301
^ From DeVries, Arthur L.; WOHLSCHLAG, Donald E. (1969). "Freezing resistance in some Antarctic fish." Science 163 (3871): 10,731,075th doi: 10.1126/science.163.3871.1073.
^ De Vries, AL, Komatsu, SK, Feeney, RE (1970). "Chemical and physical properties of freezing point depressing glycoproteins from Antarctic fishes "J Biol Chem 245 (11). 29,012,908th PMID 5488456th
^ Duman, JG, Olsen, TM (1993). "Thermal Hysteresis protein activity in bacteria, fungi and phylogenetically diverse plants, "Cryobiology 30:. 322,328th doi: 10.1006/cryo.1993.1031.
^ Ice structuring Proteins – a new name for antifreeze proteins
^ Antifreeze proteins and their genes: From basic research to business opportunity
^ Science Daily
^ Dortch, Eloise. (2006). Fishy GM yeast used to make ice. Network of Concerned Farmers. Retrieved 9th October 2006
^ Creamy, Healthier Ice Cream? What's the catch?
^ A. Regand, HD. Goff et al. (2006). Ice recrystallization inhibition in ice as affected by ice structuring proteins from winter wheat grass. J Dairy Sci. 89:1, 49-57.
^ Walters KR Jr, Serianni AS, Sformo T, Barnes BM, Duman JG (2009). "A non-protein thermal hysteresis producing antifreeze xylomannan in the frost-tolerant Alaskan Beetle Upis ceramboides "(HTML). PNAS Epub ahead of print. PMID 19,934,038th
Further Reading
Haymett, A. Ward, L., Harding, M. (1999). "Winter Flounder "antifreeze" proteins: synthesis and ice growth inhibition of analogues, the relative importance of hydrophobic interactions and hydrogen sensor "Journal the American Chemical Society 121 (5). 941 948 doi:. 10.1021/ja9801341 ISSN 00,027,863th.
Sicheri, F., Yang, DS (1995). "Ice-binding structure and mechanism of an antifreeze protein of winter flounder, "Nature 375 (6530). 427 431 doi: 10.1038/375427a0 PMID 7,760,940th ..
External Links
Cold, Hard Fact: Fish antifreeze in the pancreas produced
Categories: Proteins | Cryobiology About the Author
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