Center for Biological NMR, Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
J Phys Chem B. 2011 May 26;115(20):6653-60. doi: 10.1021/jp111448a. Epub 2011 May 2.
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable β-hairpin-α-helix structure in aqueous solutions. Molecular dynamics simulations were performed in water and methanol/water solutions using all-atom explicit models. NMR experiments were used to test the calculated results. The combined theoretical and experimental studies suggest that methanol strengthens the interactions between the polar backbone of the peptide and thus enhances the secondary structure formation; at the same time methanol weakens the hydrophobic interactions and results in an expansion of the hydrophobic core and an increase in gyration.
进行了一项组合模拟和实验研究，以研究甲醇如何影响模型肽 BBA5 的结构。BBA5 在水溶液中形成稳定的β发夹-α螺旋结构。使用全原子显式模型在水中和甲醇/水溶液中进行分子动力学模拟。NMR 实验用于测试计算结果。组合理论和实验研究表明，甲醇增强了肽的极性骨架之间的相互作用，从而增强了二级结构的形成；同时，甲醇削弱了疏水相互作用，导致疏水区扩张和回转半径增加。
