疏水氨基酸水合壳层内溶剂结构改变的直接证据。
Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid.
作者信息
Pertsemlidis A, Saxena A M, Soper A K, Head-Gordon T, Glaeser R M
机构信息
Graduate Group in Biophysics, University of California, Berkeley 94720, USA.
出版信息
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10769-74. doi: 10.1073/pnas.93.20.10769.
Neutron scattering experiments are used to determine scattering profiles for aqueous solutions of hydrophobic and hydrophilic amino acid analogs. Solutions of hydrophobic solutes show a shift in the main diffraction peak to smaller angle as compared with pure water, whereas solutions of hydrophilic solutes do not. The same difference for solutions of hydrophobic and hydrophilic side chains is also predicted by molecular dynamics simulations. The neutron scattering curves of aqueous solutions of hydrophobic amino acids at room temperature are qualitatively similar to differences between the liquid molecular structure functions measured for ambient and supercooled water. The nonpolar solute-induced expansion of water structure reported here is also complementary to recent neutron experiments where compression of aqueous solvent structure has been observed at high salt concentration.
中子散射实验用于确定疏水和亲水氨基酸类似物水溶液的散射曲线。与纯水相比，疏水溶质溶液的主要衍射峰向较小角度偏移，而亲水溶质溶液则不然。分子动力学模拟也预测了疏水和亲水侧链溶液的相同差异。室温下疏水氨基酸水溶液的中子散射曲线在定性上类似于在环境水和过冷水的液体分子结构函数之间的差异。本文报道的非极性溶质引起的水结构膨胀也与最近的中子实验互补，在该实验中，在高盐浓度下观察到了水溶剂结构的压缩。
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