中文摘要：

Phospholamban 是负责通过可逆 phosphorylation 调整 sarcoplasmic 蜂窝胃 Ca2+ 泵的活动的重要蛋白质。并且它在生活房间的三维的结构是注意的一个焦点。在当前的盒子中，我们在 phospholamban 结构上，并且在这基础、采用的长时间规模上总结了调查系统地学习它的结构的分子的动力学模拟。从在风铃草结构的 phospholamban 的一链的开始的 22 残余由 NMR 实验决定了，和它在位置 16 点的 phosphorylation，在位置 9 点的变化作为三个不同系统被拣起。由在明确的答案环境的 10 ns 的分子的动力学模拟，原来的结构的 315 残余保留了他们的螺旋结构，这被发现，当 phosphorylation 和变化有更少的概率形成螺旋结构时。这些结构的变化可能导致抑制减少到 sarcoplasmic 蜂窝胃 Ca2+ 泵，它根据以前的试验性的结果。

英文摘要：

Phospholamban is an important protein with responsibility for regulating the activity of the sarcoplasmic reticulum Ca^2＋ pump through reversible phosphorylation. And its three-dimensional structure in living cell has been a focus of attention. In the current case, we summarized the investigations on phospholamban structure, and on this base, employed long time-scale molecular dynamics simulations to study its structure systematically. The first 22 residues from one chain of phospholamban in bellflower structure determined by NMR experiments, together with its phosphorylation at position 16 and mutation at position 9 were picked up as three different systems. By molecular dynamics simulations of 10 ns in the explicit solution surroundings, it was found that the 3-15 residues of the original structure retained their helix structures, while the phosphorylation and mutation had less probability to form helix structures. These structural changes might result in inhibition decrease to the sarcoplasmic reticulum Ca^2＋ pump, which is in accordance with previous experimental results.