Kinetic model for the interaction of myosin subfragment 1 with regulated actin.
Kinetic model for the interaction of myosin subfragment 1 with regulated actin.
复制标题
肌球蛋白亚片段 1 与调节肌动蛋白相互作用的动力学模型。
DOI：
10.1016/s0006-3495(83)84286-6
复制
发表时间：
1983
影响因子：
3.4
通讯作者：
I. Epstein
中科院分区：
文献类型：
--
作者：
A. Balazs;I. Epstein
建立了一个描述肌球蛋白亚片段1（SF-1）与受调控肌动蛋白结合的一维动力学伊辛模型。该模型允许单个肌动蛋白位点与结合SF-1配体之间的合作相互作用，而不是假设肌动蛋白单体位点以合作方式改变其状态。在三重态闭合近似下，该模型产生一组16个独立的微分（主）方程，其可以数值求解以产生作为时间函数的结合程度。该模型的预测进行了比较与实验上的瞬时结合SF-1的调节肌动蛋白在Ca 2+的存在下，并在Ca 2+的情况下，与不同量的SF-1预绑定到肌动蛋白丝和SF-1 X ADP的平衡结合调节肌动蛋白在Ca 2+的情况下。在所有情况下，计算结果都在实验误差范围内拟合数据。在SF-1 × ADP的情况下，结果表明，在两个相邻的七位点肌动蛋白单元的末端相邻结合的SF-1之间存在排斥相互作用。
A one-dimensional kinetic Ising model is developed to describe the binding of myosin subfragment 1 (SF-1) to regulated actin. The model allows for cooperative interactions between individual actin sites with bound SF-1 ligands rather than assuming that groups of actin monomer sites change their state in a cooperative fashion. With the triplet closure approximation, the model yields a set of 16 independent differential (master) equations which may be solved numerically to yield the extent of binding as a function of time. The predictions of the model are compared with experiments on the transient binding of SF-1 to regulated actin in the presence of Ca2+ and in the absence of Ca2+ with varying amounts of SF-1 prebound to the actin filament and on the equilibrium binding of SF-1 X ADP to regulated actin in the absence of Ca2+. In all cases, the calculations fit the data to within the experimental errors. In the case of SF-1 X ADP, the results suggest that a repulsive interaction exists between adjacently bound SF-1 at the ends of two neighboring seven-site actin units.
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Chalovich,JM;Chock,PB;Eisenberg,E
通讯作者：
Eisenberg,E