Ca2+-dependent Antifreeze Proteins

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Antifreeze proteins

The antifreeze protein (AFP) activity is explained using two models. The first model is using ice binding and the second is using antiice structuralization of water molecules. The description of AFP function using anti-ice structuralization of water molecules is less explored. Therefore, it is of interest to explain AFP function using this model. Protein folding is often described using models ...

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Structure and Evolutionary Origin of Ca2+-Dependent Herring Type II Antifreeze Protein

In order to survive under extremely cold environments, many organisms produce antifreeze proteins (AFPs). AFPs inhibit the growth of ice crystals and protect organisms from freezing damage. Fish AFPs can be classified into five distinct types based on their structures. Here we report the structure of herring AFP (hAFP), a Ca(2+)-dependent fish type II AFP. It exhibits a fold similar to the C-ty...

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A Ca2+-dependent bacterial antifreeze protein domain has a novel beta-helical ice-binding fold.

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 ...

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A Ca2+-dependent bacterial antifreeze protein domain has a novel β-helical ice-binding fold

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-aci...

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Antifreeze proteins in Alaskan insects and spiders.

Prior to this study, antifreeze proteins (AFPs) had not been identified in terrestrial arthropods from the Arctic or anywhere in Alaska. The hemolymph of 75 species of insects and six spiders from interior and arctic Alaska were screened for thermal hysteresis (a difference between the freezing and melting points), characteristic of the presence of AFPs. Eighteen species of insects and three sp...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1996

ISSN: 0021-9258

DOI: 10.1074/jbc.271.28.16627