Patriksson Alexandra, Adams Christopher M, Kjeldsen Frank, Zubarev Roman A, van der Spoel David
J Phys Chem B. 2007 Nov 22;111(46):13147-50. doi: 10.1021/jp709901t. Epub 2007 Nov 1.
Molecular dynamics simulations of zwitterions of the Trp-cage protein in the gas phase show that the most stable ion in vacuo has preserved the charge locations acquired in solution. A direct comparison of the gas and solution-phase structures reveals that, despite the similarity in charge location, there is significant difference in the structures, with a substantial increase in hydrogen bonds and exposure of hydrophobic parts in the gas phase. The structure of the salt bridge in the gas phase is also much more stable than in the (experimental) solution structure.
气相中色氨酸笼状蛋白质两性离子的分子动力学模拟表明，真空中最稳定的离子保留了在溶液中获得的电荷位置。气相和溶液相结构的直接比较表明，尽管电荷位置相似，但结构存在显著差异，气相中氢键大量增加，疏水部分暴露。气相中盐桥的结构也比（实验）溶液结构稳定得多。
