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Titlebook: Antifreeze Proteins Volume 1; Environment, Systema Hans Raml?v,Dennis Steven Friis Book 2020 Springer Nature Switzerland AG 2020 antifreeze

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21#
發(fā)表于 2025-3-25 07:21:11 | 只看該作者
Introduction,tructuring proteins (ISPs) are a unique group of proteins that despite large differences in structure on all levels, share the common properties that they recognize, bind to, and inhibit (structure) the growth of ice crystals in cold-adapted ectothermic organisms. In the following, we will call thes
22#
發(fā)表于 2025-3-25 10:28:38 | 只看該作者
23#
發(fā)表于 2025-3-25 14:16:42 | 只看該作者
24#
發(fā)表于 2025-3-25 16:36:58 | 只看該作者
Ice Formation in Living Organismsthermic organisms. This includes the direct implication of cold “per se” on various parameters such as pH, membrane fluidity and phase transitions, ionic gradients, metabolism, cold denaturation of proteins, ice nucleation, ice growth, freezing-induced cellular dehydration, the role of aquaporins an
25#
發(fā)表于 2025-3-25 22:30:47 | 只看該作者
Fish Antifreeze Proteinstwo major types of APs, the antifreeze glycoproteins (AFGPs) found in Antarctic notothenioid fishes and northern cod fishes (gadids) and three other structurally unique small antifreeze proteins (AFPs) in unrelated taxa. Although the APs differ in composition, size, and structure, on a molar basis a
26#
發(fā)表于 2025-3-26 03:50:39 | 只看該作者
Insect Antifreeze Proteinstually exclusive, adaptations to permit survival at subzero temperatures. In general, these adaptations can be divided into those that prevent freezing of freeze susceptible species (freeze avoidance) and those that allow the insect to freeze and survive (freeze tolerance). Three types of ice-bindin
27#
發(fā)表于 2025-3-26 06:10:41 | 只看該作者
28#
發(fā)表于 2025-3-26 11:35:28 | 只看該作者
29#
發(fā)表于 2025-3-26 15:02:49 | 只看該作者
30#
發(fā)表于 2025-3-26 18:02:45 | 只看該作者
La misura delle grandezze fisiche,tructuring proteins (ISPs) are a unique group of proteins that despite large differences in structure on all levels, share the common properties that they recognize, bind to, and inhibit (structure) the growth of ice crystals in cold-adapted ectothermic organisms. In the following, we will call thes
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