Gallagher Kelly Ryan, Sharp Kim A
Department of Biochemistry and Biophysics, University of Pennsylvania, 3700 Hamilton Walk, Philadelphia, PA 19104-6059, USA.
Biophys Chem. 2003 Sep;105(2-3):195-209. doi: 10.1016/s0301-4622(03)00087-5.
The hydration of polar and apolar groups can be explained quantitatively, via the random network model of water, in terms of differential distortions in first hydration shell water-water hydrogen bonding angle. This method of analyzing solute induced structural distortions of water is applied to study the ice-binding type III thermal hysteresis protein. The analysis reveals subtle but significant differences in solvent structuring of the ice-binding surface, compared to non-ice binding protein surface. The major differences in hydration in the ice-binding region are (i). polar groups have a very apolar-like hydration. (ii). there is more uniform hydration structure. Overall, this surface strongly enhances the tetrahedral, or ice-like, hydration within the primary hydration shell. It is concluded that these two specific features of the hydration structure are important for this surface to recognize, and preferentially interact with nascent ice crystals forming in liquid water.
通过水的随机网络模型，根据第一水化层中水分子间氢键角度的差异畸变，可以定量解释极性和非极性基团的水化作用。这种分析溶质引起的水结构畸变的方法被应用于研究III型冰结合热滞蛋白。分析结果表明，与非冰结合蛋白表面相比，冰结合表面的溶剂结构存在细微但显著的差异。冰结合区域水化作用的主要差异在于：（i）极性基团具有非常类似非极性基团的水化作用。（ii）水化结构更加均匀。总体而言，该表面强烈增强了第一水化层内的四面体或类冰状水化作用。得出的结论是，水化结构的这两个特定特征对于该表面识别并优先与液态水中形成的新生冰晶相互作用很重要。
