Phillips J C, Wriggers W, Li Z, Jonas A, Schulten K
Theoretical Biophysics, Beckman Institute and Department of Physics, College of Medicine at Urbana-Champaign, University of Illinois, Urbana 61801, USA.
Biophys J. 1997 Nov;73(5):2337-46. doi: 10.1016/S0006-3495(97)78264-X.
In reconstituted high-density lipoproteins, apolipoprotein A-I and phosphatidylcholines combine to form disks in which the amphipathic alpha-helices of apolipoprotein A-1 bind to the edge of a lipid bilayer core, shielding the hydrophic lipid tails from the aqueous environment. We have employed experimental data, sequence analysis, and molecular modeling to construct an atomic model of such a reconstituted high-density lipoprotein disk consisting of two apolipoprotein A-I proteins and 160 palmitoyloleoylphosphatidylcholine lipids. The initial globular domain (1-47) of apolipoprotein A-I was excluded from the model, which was hydrated with an 8-A shell of water molecules. Molecular dynamics and simulated annealing were used to test the stability of the model. Both head-to-tail and head-to-head forms of a reconstituted high-density lipoprotein were simulated. In our simulations the protein contained and adhered to the lipid bilayer while providing good coverage of the lipid tails.
在重组高密度脂蛋白中，载脂蛋白A-I和磷脂酰胆碱结合形成盘状结构，其中载脂蛋白A-1的两亲性α螺旋与脂质双层核心的边缘结合，使疏水的脂质尾部与水性环境隔离。我们利用实验数据、序列分析和分子建模构建了一个由两个载脂蛋白A-I蛋白和160个棕榈酰油酰磷脂酰胆碱脂质组成的重组高密度脂蛋白盘的原子模型。载脂蛋白A-I的初始球状结构域（1-47）被排除在模型之外，该模型用水分子的8埃壳层进行水合。分子动力学和模拟退火被用于测试模型的稳定性。模拟了重组高密度脂蛋白的头对头和头对尾形式。在我们的模拟中，蛋白质包含并附着在脂质双层上，同时对脂质尾部提供了良好的覆盖。
