Insight into a molecular interaction force supporting peptide backbones and its implication to protein loops and folding.
Insight into a molecular interaction force supporting peptide backbones and its implication to protein loops and folding.
复制标题
洞察一种新的分子相互作用力及其对蛋白质环和折叠的影响。
DOI：
10.1080/07391102.2014.984333
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发表时间：
2015-09
影响因子：
4.4
通讯作者：
Chou KC
中科院分区：
文献类型：
--
作者：
Du QS;Chen D;Xie NZ;Huang RB;Chou KC
虽然环段不像α-螺旋和β-链那样被归类为最基本的蛋白质结构元件，但它可能在蛋白质的稳定性、灵活性和动态活性方面发挥着相当大的作用。与此同时，蛋白质环也非常难以捉摸；即它与蛋白质其他部分的相互作用以及它自己的形状保持力仍然是一个谜，或者至少还不是很清楚。在这里，我们报告了一种分子力，即所谓的极性氢-π相互作用(HP-π)，它可能在支持蛋白质环的骨架方面发挥重要作用。通过在多肽键单元的准π平面上进行势能面扫描计算，我们观察到了以下有趣的现象：(1)当一个多肽单元的极性氢原子垂直指向其他多肽键单元的π平面时，发生了显著的HP-π相互作用；(2)这种相互作用是距离和取向相关的，作用空间很广，属于‘点对面’相互作用。这里报道的分子力可能为更好地理解环的独特稳定性和灵活性特征以及蛋白质全球折叠的驱动力提供有用的相互作用概念和见解。
Although not being classified as the most fundamental protein structural elements like α-helices and β-strands, the loop segment may play considerable roles for protein stability, flexibility, and dynamic activity. Meanwhile, the protein loop is also quite elusive; i.e. its interactions with the other parts of protein as well as its own shape-maintaining forces have still remained as a puzzle or at least not quite clear yet. Here, we report a molecular force, the so-called polar hydrogen–π interaction (Hp–π), which may play an important role in supporting the backbones of protein loops. By conducting the potential energy surface scanning calculations on the quasi π-plane of peptide bond unit, we have observed the following intriguing phenomena: (1) when the polar hydrogen atom of a peptide unit is perpendicularly pointing to the π-plane of other peptide bond units, a remarkable Hp–π interaction occurs; (2) the interaction is distance and orientation dependent, acting in a broad space, and belonging to the ‘point-to-plane’ one. The molecular force reported here may provide useful interaction concepts and insights into better understanding the loop’s unique stability and flexibility feature, as well as the driving force of the protein global folding.