Kinetics of actin-myosin binding. I. An exactly soluble one-variable model.

Kinetics of actin-myosin binding. I. An exactly soluble one-variable model.
复制标题

肌动蛋白-肌球蛋白结合的动力学。

DOI:
10.1016/s0006-3495(87)83329-5
复制
发表时间:
1987
影响因子:
3.4
通讯作者:
Epstein,IR
Epstein,IR
中科院分区:
生物学3区
文献类型:
--
作者:
Klonowski,W;Epstein,IR

文献摘要

被引文献

相似文献

为了尽可能简单地处理肌动蛋白-肌球蛋白结合的动力学,开发了一个单变量模型,并引入了有效因子的概念。有效性因子是存在协同性时的反应速率与不存在协同性时的反应速率之比,通过对属于一个七位点肌动蛋白单位的所有位点的协同性因子取平均值来计算。该技术适用于各种模型,涉及合作协会和解离过程。这种平均假设所有受调节的肌动蛋白单位都是等价的。该模型可以精确地解决任意程度的“预加载”的亚片段1(S1)的调节肌动蛋白。
To treat the kinetics of actin-myosin binding as simply as possible, a one-variable model is developed and the notion of effectivity factors is introduced. An effectivity factor is a ratio of the reaction rate in the presence of cooperativity to that in the noncooperative case and is calculated by averaging cooperativity factors over all sites belonging to one seven-site actin unit. The technique is applicable to a variety of models involving cooperative association and dissociation processes. This averaging assumes the equivalence of all regulated actin units. The model may be solved exactly for arbitrary degrees of "preloading" of subfragment 1 (S1) on the regulated actin.