论文标题
H键在Crambin：Alpha Helix中的连贯性
H-bonds in Crambin: Coherence in an alpha helix
论文作者
论文摘要
我们将相干分析应用于植物蛋白crambin的分子动力学模拟，植物蛋白crambin是一种在阿比西尼亚白菜中发现的硫蛋白储存蛋白。工程师开发了一致性分析，以识别无统计假设的线性相互作用。在0.391 GHz和5.08 GHz之间的Alpha螺旋中的氧和H键的氧气位移与H键的氮原子的位移之间大于0.9（相对于2.56 ns和0.197 ns的时间）。这些H键的作用很像线性系统。无关的原子具有不相关的动作和较小的连贯性，例如0.02。将原子组（该组形成α螺旋层）平均，并评估两组的相干函数。 Alpha螺旋的层形成线性系统，表明经典分子动力学的谐波分析可以成功地描述Alpha螺旋层的变构相互作用。
We applied coherence analysis to molecular dynamics simulations of the plant protein crambin, a thionin storage protein found in Abyssinian cabbage. Coherence analysis was developed by engineers to identify linear interactions, without statistical assumptions. Coherence is greater than 0.9 between the displacement of oxygen and nitrogen atoms of H bonds in alpha helices for frequencies between 0.391 GHz and 5.08 GHz (corresponding reciprocally to times of 2.56 ns and 0.197 ns). These H bonds act much like a linear system. Unrelated atoms have uncorrelated motions and much smaller coherence, say 0.02. Groups of atoms (that form a layer of an alpha helix) were averaged and the coherence function of two groups was evaluated. Layers of the alpha helix form a linear system, suggesting that the harmonic analysis of classical molecular dynamics can successfully describe the allosteric interactions of the layers of an alpha helix.
