抗冻蛋白action的机制，基于水和新的“亲簇”相互作用的层次理论
Mechanism of antifreeze proteins action, based on Hierarchic theory of water and new ''clusterphilic'' interaction
摘要：
一个基本上是新的层次理论，一般用于固体和液体（Kaivarainen，2001年，2000年，1995年，1992年），已简要描述和说明的例子水和冰的计算机模拟。洛斯-阿拉莫斯arXiv的系列文章（见http：//arXiv.org/abs/physics/0102086）提供了理论及其众多应用的完整描述。新的亲簇相互作用，亲水性和疏水性之间的中间，介绍。它们可细分为：分子内-当水簇位于大的域间或亚基间空腔和分子间亲簇相互作用的“开放"状态时。分子间亲簇相互作用可以由非常不同的大分子诱导。后者主要表现为大分子与水分子团簇的结合，形成所谓的“团簇”。亲脂性相互作用在生物系统的自组织中起着重要作用，特别是多球变构酶、微管和肌动蛋白丝。选择文献综述，致力于抗冻蛋白（AFP）和冰核蛋白（INP）与水的相互作用。基于层次理论对相应的实验结果进行了分析。提出了低温蛋白影响水的凝固点的可能机理。文中还介绍了AFP作用新模型的结果及其实验验证的途径。
英文摘要：
A basically new Hierarchic theory, general for solids and liquids (Kaivarainen, 2001, 2000, 1995, 1992), has been briefly described and illustrated by computer simulations on examples of water and ice. Full description of theory and its numerous applications are presented in series of articles at the arXiv of Los-Alamos (see http://arXiv.org/abs/physics/0102086). New clusterphilic interactions, intermediate between hydrophilic and hydrphobic, are introduced. They can be subdivided into: intramolecular - when water cluster is localized in the ''open'' states of big interdomain or intersubunit cavities and intermolecular clusterphilic interactions. Intermolecular clusterphilic interactions can be induced by very different macromolecules. The latter displays themselves in bordering of water cluster by macromolecules and forming so-called ''clustrons''. Clusterphilic interactions can play an important role in self-organization of biosystems, especially multiglobular allosteric enzymes, microtubules and the actin filaments. The selected review of literature, devoted to antifreeze proteins (AFP) and ice-nucleation proteins (INP) interaction with water is presented. Corresponding experimental results were analyzed on the base of Hierarchic theory. The possible mechanism of cryoproteins influence on water, changing its freezing point has been proposed. The consequences of new model of AFP action and ways of its experimental verification are described also.
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