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Relevant bibliographies by topics / Hyperactive antifreeze proteins

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Academic literature on the topic 'Hyperactive antifreeze proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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Journal articles on the topic "Hyperactive antifreeze proteins"

1

Stein, Benjamin P. "Hyperactive antifreeze proteins." Physics Today 60, no. 5 (May 2007): 24. http://dx.doi.org/10.1063/1.4796425.

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2

Graham, Laurie A., Wensheng Qin, Stephen C. Lougheed, Peter L. Davies, and Virginia K. Walker. "Evolution of Hyperactive, Repetitive Antifreeze Proteins in Beetles." Journal of Molecular Evolution 64, no. 4 (April 2007): 387–98. http://dx.doi.org/10.1007/s00239-005-0256-3.

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3

Drori, Ran, Yeliz Celik, Peter L. Davies, and Ido Braslavsky. "144 Kinetics of hyperactive and moderate antifreeze proteins." Cryobiology 67, no. 3 (December 2013): 439. http://dx.doi.org/10.1016/j.cryobiol.2013.09.150.

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4

Drori, Ran, Yeliz Celik, Peter L. Davies, and Ido Braslavsky. "Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics." Journal of The Royal Society Interface 11, no. 98 (September 6, 2014): 20140526. http://dx.doi.org/10.1098/rsif.2014.0526.

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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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5

Garnham, Christopher P., Jack A. Gilbert, Christopher P. Hartman, Robert L. Campbell, Johanna Laybourn-Parry, and Peter L. Davies. "A Ca2+-dependent bacterial antifreeze protein domain has a novel β-helical ice-binding fold." Biochemical Journal 411, no. 1 (March 13, 2008): 171–80. http://dx.doi.org/10.1042/bj20071372.

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AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large (>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned, expressed and characterized a 322-amino-acid region of the protein where the antifreeze activity is localized that shows similarity to the RTX (repeats-in-toxin) family of proteins. The recombinant protein requires Ca2+ for structure and activity, and it is capable of depressing the freezing point of a solution in excess of 2 °C at a concentration of 0.5 mg/ml, therefore classifying it as a hyperactive AFP. We have developed a homology-guided model of the antifreeze region based partly on the Ca2+-bound β-roll from alkaline protease. The model has identified both a novel β-helical fold and an ice-binding site. The interior of the β-helix contains a single row of bound Ca2+ ions down one side of the structure and a hydrophobic core down the opposite side. The ice-binding surface consists of parallel repetitive arrays of threonine and aspartic acid/asparagine residues located down the Ca2+-bound side of the structure. The model was tested and validated by site-directed mutagenesis. It explains the Ca2+-dependency of the region, as well its hyperactive antifreeze activity. This is the first bacterial AFP to be structurally characterized and is one of only five hyperactive AFPs identified to date.

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6

Bar-Dolev, Maya, Yeliz Celik, J. S. Wettlaufer, Peter L. Davies, and Ido Braslavsky. "New insights into ice growth and melting modifications by antifreeze proteins." Journal of The Royal Society Interface 9, no. 77 (July 11, 2012): 3249–59. http://dx.doi.org/10.1098/rsif.2012.0388.

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Antifreeze proteins (AFPs) evolved in many organisms, allowing them to survive in cold climates by controlling ice crystal growth. The specific interactions of AFPs with ice determine their potential applications in agriculture, food preservation and medicine. AFPs control the shapes of ice crystals in a manner characteristic of the particular AFP type. Moderately active AFPs cause the formation of elongated bipyramidal crystals, often with seemingly defined facets, while hyperactive AFPs produce more varied crystal shapes. These different morphologies are generally considered to be growth shapes. In a series of bright light and fluorescent microscopy observations of ice crystals in solutions containing different AFPs, we show that crystal shaping also occurs during melting. In particular, the characteristic ice shapes observed in solutions of most hyperactive AFPs are formed during melting. We relate these findings to the affinities of the hyperactive AFPs for the basal plane of ice. Our results demonstrate the relation between basal plane affinity and hyperactivity and show a clear difference in the ice-shaping mechanisms of most moderate and hyperactive AFPs. This study provides key aspects associated with the identification of hyperactive AFPs.

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7

Mochizuki, Kenji, and Masakazu Matsumoto. "Collective Transformation of Water between Hyperactive Antifreeze Proteins: RiAFPs." Crystals 9, no. 4 (April 1, 2019): 188. http://dx.doi.org/10.3390/cryst9040188.

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We demonstrate, by molecular dynamics simulations, that water confined between a pair of insect hyperactive antifreeze proteins from the longhorn beetle Rhagium inquisitor is discontinuously expelled as the two proteins approach each other at a certain distance. The extensive striped hydrophobic–hydrophilic pattern on the surface, comprising arrays of threonine residues, enables water to form three independent ice channels through the assistance of hydroxyl groups, even at 300 K. The transformation is reminiscent of a freezing–melting transition rather than a drying transition and governs the stable protein–protein separation in the evaluation of the potential of mean force. The collectivity of water penetration or expulsion and the hysteresis in the time scale of ten nanoseconds predict a potential first-order phase transition at the limit of infinite size and provide a new framework for the water-mediated interaction between solutes.

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8

Kristiansen, Erlend, Casper Wilkens, Bjarne Vincents, Dennis Friis, Anders Blomkild Lorentzen, Håvard Jenssen, Anders Løbner-Olesen, and Hans Ramløv. "Hyperactive antifreeze proteins from longhorn beetles: Some structural insights." Journal of Insect Physiology 58, no. 11 (November 2012): 1502–10. http://dx.doi.org/10.1016/j.jinsphys.2012.09.004.

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9

Meister, K., S. Ebbinghaus, Y. Xu, J. G. Duman, A. DeVries, M. Gruebele, D. M. Leitner, and M. Havenith. "Long-range protein-water dynamics in hyperactive insect antifreeze proteins." Proceedings of the National Academy of Sciences 110, no. 5 (December 31, 2012): 1617–22. http://dx.doi.org/10.1073/pnas.1214911110.

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10

Mizrahy, Ortal, Maya Bar, and Ido Braslavsky. "115. Enhancing the activity of hyperactive antifreeze proteins with additives." Cryobiology 63, no. 3 (December 2011): 338. http://dx.doi.org/10.1016/j.cryobiol.2011.09.118.

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More sources

Dissertations / Theses on the topic "Hyperactive antifreeze proteins"

1

Choi, Young Eun. "A Study on the Hyperactive Antifreeze Proteins from the Insect Tenebrio molitor." Ohio : Ohio University, 2007. http://www.ohiolink.edu/etd/view.cgi?ohiou1195953014.

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2

Bu, Sen. "Modification, Expression, and Purification of Hyperactive Antifreeze Proteins from Insect Tenebrio Molitor." Cleveland State University / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=csu1328667906.

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3

Celik, Yeliz. "Experimental Investigation of the Interactions of Hyperactive Antifreeze Proteins with Ice Crystals." Ohio University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1268166115.

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