The basis of the hydrophobic effect
The basis of the hydrophobic effect
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DOI：
10.1016/s0301-4622(02)00281-8
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发表时间：
2003-01-01
影响因子：
3.8
通讯作者：
Kyte, J
中科院分区：
文献类型：
--
作者：
Kyte, J
最可靠地决定其将经历的疏水效应大小的分子特性是其包含的氢碳键的数量，而不是其非极性部分的可及表面积。这一结论是通过对烷烃、烯烃、链二烯和芳烃从水转移到十六烷的标准自由能的检查得出的。当将这些不同类别的碳氢化合物的标准转移自由能绘制为它们所含氢碳键数量的函数时，所有数据都落在同一条线上。这些标准转移自由能也与碳氢化合物所含的氢碳键数量成正比。当将相同的标准转移自由能绘制为烃的可及表面积的函数时，数据不会落在同一条线上，标准转移自由能也不与可及表面积成正比。对不同类别碳氢化合物从气相到水以及从气相到十六烷的标准转移自由能的检查强化了这样的结论：分子中氢碳键的数量而不是其可及的表面积是疏水效应的基础。因此，估计不同官能团对提供蛋白质分子折叠自由能或提供两个蛋白质缔合或配体与蛋白质缔合的解离自由能的疏水效应的贡献应通过计算排除在水中的氢碳键的数量而不是计算排除在水中的可及表面积来进行。 (C) 2002 Elsevier Science B.V. 保留所有权利。
The property of a molecule that most reliably determines the magnitude of the hydrophobic effect that it will experience is the number of hydrogen-carbon bonds it contains not the accessible surface area of its nonpolar portions. This conclusion follows from an examination of the standard free energies of transfer of alkanes, alkenes, alkadienes, and arenes from water to hexadecane. When the standard free energies of transfer for hydrocarbons in these different classes are plotted as a function of the number of hydrogen-carbon bonds they contain, all of the data fall upon the same line. These standard free energies of transfer are also directly proportional to the number of hydrogen-carbon bonds the hydrocarbons contain. When the same standard free energies of transfer are plotted as a function of the accessible surface areas of the hydrocarbons, the data do not fall upon the same line nor are the standard free energies of transfer directly proportional to the accessible surface areas. An examination of the standard free energies of transfer for the different classes of hydrocarbons from the gas phase to water and from the gas phase to hexadecane reinforces the conclusion that the number of hydrogen-carbon bonds in a molecule rather than its accessible surface area is the basis of the hydrophobic effect. Consequently, estimates of the contribution of different functional groups to the hydrophobic effect providing the free energy of folding of a molecule of protein or providing the free energy of dissociation for the association of two proteins or the association of a ligand with a protein should be made by counting the number of hydrogen-carbon bonds excluded from water rather than computing the accessible surface areas excluded from water. (C) 2002 Elsevier Science B.V. All rights reserved.