Long-range protein-water dynamics in hyperactive insect antifreeze proteins
Long-range protein-water dynamics in hyperactive insect antifreeze proteins
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DOI：
10.1073/pnas.1214911110
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发表时间：
2013-01-29
影响因子：
11.1
通讯作者：
Havenith, Martina
中科院分区：
文献类型：
--
作者：
Meister, Konrad;Ebbinghaus, Simon;Havenith, Martina
抗冻蛋白（AFP）是能够降低水溶液相对于熔点的冰点的特定蛋白质。在昆虫中发现的高度活跃的 AFP 具有特别高的降低冰点的能力，远远超过其他 AFP 的能力。在之前的研究中，我们假设AFP的活性可归因于两种不同的分子机制：（i）蛋白质表面与不断增长的冰面的短程直接相互作用和（ii）蛋白质诱导的水动力学从蛋白质表面延伸至20埃的长程相互作用。在本文中，我们结合太赫兹光谱和分子模拟来证明长程蛋白质-水相互作用对来自加拿大树突甲虫的昆虫 AFP 的高抗冻活性做出了重要贡献。我们还通过研究添加渗透剂柠檬酸钠的影响来支持我们的假设。
Antifreeze proteins (AFPs) are specific proteins that are able to lower the freezing point of aqueous solutions relative to the melting point. Hyperactive AFPs, identified in insects, have an especially high ability to depress the freezing point by far exceeding the abilities of other AFPs. In previous studies, we postulated that the activity of AFPs can be attributed to two distinct molecular mechanisms: (i) short-range direct interaction of the protein surface with the growing ice face and (ii) long-range interaction by protein-induced water dynamics extending up to 20 angstrom from the protein surface. In the present paper, we combine terahertz spectroscopy and molecular simulations to prove that long-range protein-water interactions make essential contributions to the high antifreeze activity of insect AFPs from the beetle Dendroides canadensis. We also support our hypothesis by studying the effect of the addition of the osmolyte sodium citrate.