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Protein hydration

机译：蛋白质水合

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A hydration shell surrounds proteins in solution. The structures of proteins at atomic resolution presently available in the Protein Data Bank (PDB) provide detailed information on the mode of hydration and plausible roles of water molecules in protein structure and function. This article presents an analysis of water structure in proteins determined at atomic resolution. Water molecules bind to proteins by making hydrogen bonds with oxygen and nitrogen atoms with oxygen as the preferred atom. The mean length of hydrogen bonds between oxygen and water is shorter than that of nitrogen and water. However, the mean thermal parameter of water molecules hydrogen-bonded to oxygen atoms is higher than that of water molecules hydrogen-bonded to nitrogen atoms. Water molecules of the first hydration shell are stabilized by hydrogen bonding with protein atoms, while the stability of the second hydration shell is derived from hydrogen bonding with molecules of the first shell. The number of molecules in the second and higher shells is less than half of that of the first shell. As could be expected, the mean thermal parameter of molecules is higher in the second shell compared to that of the first shell. The number of water molecules buried in protein interfaces increases with increasing size of protein. In several proteins, water molecules form hydrogen-bonded networks that could cover a large part of the protein surface. Pentagonal and tetrahedral arrangements of hydrogen-bonded water molecules could be observed in several structures. Strongly bound water molecules with low thermal parameters appear to be essential for maintaining the loops in appropriate positions. Tightly bound water molecules are also found at the active site of some proteins. These molecules may play important roles in protein function.
机译：溶液中的蛋白质周围有一个水合壳。蛋白质数据库（PDB）中现有的蛋白质原子分辨率结构提供了水化模式的详细信息，以及水分子在蛋白质结构和功能中可能发挥的作用。本文介绍了在原子分辨率下测定蛋白质中水结构的分析。水分子通过与氧和氮原子形成氢键与蛋白质结合，氧是首选原子。氧和水之间氢键的平均长度比氮和水短。然而，与氧原子氢键结合的水分子的平均热参数高于与氮原子氢键结合的水分子的平均热参数。第一水合壳的水分子通过与蛋白质原子的氢键而稳定，而第二水合壳的稳定性则来自与第一水合壳的分子的氢键。第二层和更高层的分子数量不到第一层的一半。正如所料，第二层分子的平均热参数高于第一层分子的平均热参数。埋藏在蛋白质界面的水分子数量随着蛋白质大小的增加而增加。在一些蛋白质中，水分子形成氢键网络，可以覆盖蛋白质表面的大部分。氢键水分子的五边形和四面体排列可以在几种结构中观察到。具有低热参数的强束缚水分子似乎对维持环在适当位置至关重要。在某些蛋白质的活性部位也发现了紧密结合的水分子。这些分子可能在蛋白质功能中发挥重要作用。

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