Role of hydration force in the self-assembly of collagens and amyloid steric zipper filaments.
Role of hydration force in the self-assembly of collagens and amyloid steric zipper filaments.
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DOI：
10.1021/ja204377y
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发表时间：
2011-08-03
影响因子：
15
通讯作者：
Hwang, Wonmuk
中科院分区：
文献类型：
--
作者：
Ravikumar, Krishnakumar M.;Hwang, Wonmuk
在蛋白质自组装中，表面的类型决定了它们之间的力。然而，周围的水在多大程度上有助于这种力量仍然是一个基本问题。在这里，我们研究了三个自组装细丝系统，分别有水合（胶原），干燥的非极性和干燥的极性（淀粉样蛋白）接口。使用分子动力学模拟，我们计算和比较当地的水化地图和水化力。我们发现，初级水化壳形成的表面，无论潜在的氨基酸的类型。弱振荡的水化力产生的合并和耗尽的水化壳作为两个长丝的方法，而当地的水扩散，取向，或氢键的事件没有直接的影响。水合，极性和非极性界面之间的水合力在相对于平衡表面分离的振荡的振幅和相位上不同。因此，水介导的这些蛋白质表面之间的相互作用，从“疏水性”到“亲水性”的字符范围内，有一个共同的分子起源的基础上形成的强大的水化壳，这是可能适用于广泛的生物分子组装体的界面几何形状是相似的长度尺度本研究。
In protein self-assembly, types of surfaces determine the force between them. Yet the extent to which the surrounding water contributes to this force remains as a fundamental question. Here we study three self-assembling filament systems that respectively have hydrated (collagen), dry non-polar and dry polar (amyloid) interfaces. Using molecular dynamics simulations, we calculate and compare local hydration maps and hydration forces. We find that the primary hydration shells are formed all over the surface, regardless of the types of the underlying amino acids. The weakly oscillating hydration force arises from coalescence and depletion of hydration shells as two filaments approach, whereas local water diffusion, orientation, or hydrogen bonding events have no direct effect. Hydration forces between hydrated, polar, and non-polar interfaces differ in the amplitude and phase of the oscillation relative to the equilibrium surface separation. Therefore, water-mediated interactions between these protein surfaces ranging in character from `hydrophobic' to `hydrophilic,' have a common molecular origin based on the robustly formed hydration shells, which is likely applicable to a broad range of biomolecular assemblies whose interfacial geometry is similar in length scale to those of the present study.
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影响因子：
3.9
作者：
Besseling, NAM
通讯作者：
Besseling, NAM
影响因子：
15
作者：
DELOOF, H;NILSSON, L;RIGLER, R
通讯作者：
RIGLER, R
DOI：
10.1073/pnas.212637899
发表时间：
2002-12-10
影响因子：
11.1
作者：
Fenimore, PW;Frauenfelder, H;Parak, FG
通讯作者：
Parak, FG
影响因子：
3.4
作者：
Despa, Florin;Berry, R. Stephen
通讯作者：
Berry, R. Stephen
影响因子：
4.4
作者：
Bussi, Giovanni;Donadio, Davide;Parrinello, Michele
通讯作者：
Parrinello, Michele