Häussler Wolfgang
FRM-II & E21, Technische Universität München, Garching, Germany.
Eur Biophys J. 2008 Jun;37(5):563-71. doi: 10.1007/s00249-008-0262-7. Epub 2008 Feb 13.
The dynamics of proteins are often studied by means of quasielastic neutron scattering (QENS), for example by time-of-flight methods. The spatial dimensions (10-20 nm) present in protein solutions are accessible by neutron scattering. In this article, a systematic study of diffusive dynamics of ferritin and apoferritin (=ferritin without iron core) is presented. Apoferritin consists of a spherical shell built of 24 protein units and carries net negative charge at pH 5. We have studied diffusive dynamics of ferritin solutions by neutron spin echo (NSE). We pay attention to an important feature of this technique compared to other QENS methods, which being the usage of a broad wavelength band. Using a more sophisticated fit function than usually used in NSE, we find as expected in low concentrated systems that the diffusion coefficient approaches the free-particle value of apoferritin and coincides with the diameter of the apoferritin shell (12.2 nm). In interacting solutions, the NSE results reveal that the dynamic picture of this complex liquid is dominated by slowing down of the dynamics. In low-salt solutions, a structure factor peak appears due to ordering of the ferritin molecules on the length scale of several intermolecular distances. We discuss the usage of different NSE fit functions for interacting solutions near the structure factor peak. Comparison of the dependence of elastic and dynamic data on the scattering vector value shows the influence of indirect interactions on the dynamic picture, irrespective of the way of data analysis, which being necessary due to the broad wavelength spectrum.
蛋白质动力学通常通过准弹性中子散射(QENS)来研究,例如采用飞行时间方法。蛋白质溶液中存在的空间维度(10 - 20纳米)可通过中子散射来获取。本文对铁蛋白和脱铁铁蛋白(= 不含铁芯的铁蛋白)的扩散动力学进行了系统研究。脱铁铁蛋白由24个蛋白质单元构成的球壳组成,在pH值为5时带有净负电荷。我们通过中子自旋回波(NSE)研究了铁蛋白溶液的扩散动力学。与其他QENS方法相比,我们关注该技术的一个重要特征,即使用宽波段波长。使用比NSE中通常使用的更复杂的拟合函数,我们发现在低浓度系统中,扩散系数如预期那样接近脱铁铁蛋白的自由粒子值,并且与脱铁铁蛋白壳的直径(12.2纳米)一致。在相互作用的溶液中,NSE结果表明这种复杂液体的动力学图景主要由动力学减慢主导。在低盐溶液中,由于铁蛋白分子在几个分子间距离的长度尺度上有序排列,出现了一个结构因子峰。我们讨论了在结构因子峰附近的相互作用溶液中不同NSE拟合函数的使用。弹性和动态数据对散射矢量值的依赖性比较表明,间接相互作用对动力学图景有影响,无论数据分析方式如何,由于宽波长谱这都是必要的。