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A peek at ice binding by antifreeze proteins

机译：窥视防冻蛋白与冰的结合

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摘要

What is the toughest recognition problem in biology? Arguably, it is that faced by antifreeze or thermal hysteresis proteins. These proteins provide a broad range of organisms with protection against freezing damage by depressing, in a noncolligative manner, the freezing point of water. They do this by binding to nascent ice nuclei and inhibiting their growth (1). In other words, antifreeze proteins (AFPs) must distinguish one phase of water, ice, from another phase, liquid. Moreover, the latter is present in great excess at 55 M. There are no chemical differences to key off, just the subtle structural differences, still poorly characterized, that exist between the surface of ice nuclei and liquid water. In addition to the intrinsic interest of the ice recognition problem, AFPs have application to cryo-preservation of tissues and organs (2) and to the food industry (3).
机译：生物学中最棘手的识别问题是什么？可以说，它是抗冻蛋白或热滞后蛋白所面临的问题。这些蛋白质通过非冲突方式降低水的冰点，从而为广泛的生物提供了防止冰冻损害的保护作用。它们通过与新生的冰核结合并抑制其生长来做到这一点（1）。换句话说，防冻蛋白（AFP）必须将水​​，冰的一相与液体的另一相区分开。而且，后者在55 M时大量过量存在。没有能消除的化学差异，只是冰核表面和液态水之间存在的细微结构差异（仍很差）。除了对冰识别问题的内在兴趣外，AFP还应用于组织和器官的冷冻保存（2）和食品工业（3）。

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