Intermolecular interaction of actin revealed by a dynamic light scattering technique.
Intermolecular interaction of actin revealed by a dynamic light scattering technique.
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通过动态光散射技术揭示肌动蛋白的分子间相互作用。
DOI：
10.1021/jp054865g
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
K. Onuma
中科院分区：
文献类型：
--
作者：
N. Kanzaki;T. Uyeda;K. Onuma
用动态光散射技术研究了肌动蛋白分子间的相互作用力。在含有0 - 10 mM低浓度KCl的G-缓冲液中，准确测定单体肌动蛋白的相互扩散系数（D）。（87 +/- 3）x 10（-12）m（2）.s（-1），在25 ℃和pH 7.4下，其给出单体肌动蛋白的流体动力学半径r（H）= 2.8 +/- 0.1 nm。Derjaguin-Landau-Verwey-Overbeek（DLVO）理论假设了静电势和货车德瓦尔斯势，但未能描述相互作用参数（λ）随KCl浓度的变化，而扩展的DLVO理论则成功地假设了一个额外的排斥势。首次测定了肌动蛋白在Ca（2+）-ATP结合状态下的Hamaker常数A（H）= 10.4 +/- 0.6 k（B）T。
The intermolecular interaction force of actin was studied by a dynamic light scattering technique. The mutual diffusion coefficients (D) of monomeric actin were accurately determined in a G-buffer with a low concentration of KCl from 0 to 10 mM. The translational diffusion coefficient was obtained as D(0) = (87 +/- 3) x 10(-12) m(2).s(-1) at 25 degrees C and pH 7.4, which gives a hydrodynamic radius of monomeric actin of r(H) = 2.8 +/- 0.1 nm. The Derjaguin-Landau-Verwey-Overbeek (DLVO) theory, assuming electrostatic and van der Waals potentials, failed to describe the change in interaction parameter (lambda) with KCl concentration, but the extended DLVO theory succeeded if an additional repulsive potential was assumed. The Hamaker constant of actin in the Ca(2+)-ATP bound state was determined for the first time as A(H) = 10.4 +/- 0.6 k(B)T.