Irisa M
Department of Biochemical engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, 680-4 Kawazu, Iizuka-city, Fukuoka, 820-8502 Japan.
J Biol Phys. 2002 Sep;28(3):347-57. doi: 10.1023/A:1020352303294.
One of the interactions between macromolecules is the attractive forcethrough the excluded volume effect. We studied the attraction betweenthe molecules of muscle protein, actin, in the two points by using theextended scaled particle theory (XSPT). I) we verified the basic assumptionused in the XSPT that topological elements which determine the analyticalexpression of the excluded volume are almost unchanged through the scalingdown of the solute molecule in the thought experiment. Results of thecomputational geometry method (α-shape method) showed that thisassumption is valid even in the case of the actin molecule. II) wecalculated the attraction between actin monomer molecules, G-actin.Calculated differences of the values of the attraction potential of twomacromolecules between at contact and at one macromolecule apart by theXSPT is almost the same as those by the Asakura-Oosawa theory.
大分子之间的相互作用之一是通过排除体积效应产生的吸引力。我们使用扩展标度粒子理论(XSPT)研究了肌肉蛋白肌动蛋白分子两点之间的吸引力。I)我们验证了XSPT中使用的基本假设,即在思想实验中,决定排除体积解析表达式的拓扑元素几乎不会随着溶质分子的缩小而改变。计算几何方法(α形状法)的结果表明,即使在肌动蛋白分子的情况下,这一假设也是有效的。II)我们计算了肌动蛋白单体分子(G-肌动蛋白)之间的吸引力。通过XSPT计算得出的两个大分子在接触时和相距一个大分子时吸引力势值的差异与朝仓-大泽理论计算得出的差异几乎相同。