Laboratorium für Physikalische Chemie, ETH-Zentrum, Universitätsstrasse 22, CH-8092, Zürich, Switzerland.
J Biomol NMR. 1996 Dec;8(4):453-76. doi: 10.1007/BF00228147.
The influence of water binding on the conformational dynamics of the cyclic decapeptide antamanide dissolved in the model lipophilic environment chloroform is investigated by NMR relaxation measurements. The water-peptide complex has a lifetime of 35 μs at 250 K, which is longer than typical lifetimes of water-peptide complexes reported in aqueous solution. In addition, there is a rapid intracomplex mobility that probably involves librational motions of the bound water or water molecules hopping between different binding sites. Water binding restricts the flexibility of antamanide. The experimental findings are compared with GROMOS molecular dynamics simulations of antamanide with up to eight bound water molecules. Within the simulation time of 600 ps, no water molecule leaves the complex. Additionally, the simulations show a reduced flexibility for the complex in comparison with uncomplexed antamanide. Thus, there is a qualitative agreement between the experimental NMR results and the computer simulations.
通过 NMR 弛豫测量研究了水合作用对溶解在模型亲脂环境氯仿中的环状十肽抗真菌肽构象动力学的影响。在 250 K 时，水-肽复合物的寿命为 35 μs，比在水溶液中报道的典型水-肽复合物的寿命长。此外，还有一种快速的内复合物迁移，可能涉及结合水的摆动运动或水分子在不同结合位点之间跳跃。水合作用限制了抗真菌肽的柔韧性。实验结果与多达 8 个结合水的 GROMOS 分子动力学模拟的抗真菌肽进行了比较。在 600 ps 的模拟时间内，没有水分子离开复合物。此外，与未复合的抗真菌肽相比，模拟显示复合物的柔韧性降低。因此，实验 NMR 结果与计算机模拟之间存在定性一致性。
