Hill T L
Proc Natl Acad Sci U S A. 1980 Aug;77(8):4803-7. doi: 10.1073/pnas.77.8.4803.
Wegner's theory of steady-state head-to-tail polymerization of actin (or microtubules) is extended somewhat in order to show the explicit role of the ATP (or GTP) free energy of hydrolysis (X) in the steady-state kinetics. The monomer flux and the ATP flux can both be expressed in terms of X and rate constants of the model. Both fluxes approach zero as X leads to 0 (by variation of the concentrations of ATP, ADP, and Pi); this limit corresponds to ATP equilibrium. The dependence of rate constants on these concentrations is examined. Free energy levels of the monomer kinetic cycle and the rate of free energy dissipation are discussed. The steady-state polymer length distribution is derived for a special case.
为了说明水解的ATP(或GTP)自由能(X)在稳态动力学中的明确作用,韦格纳关于肌动蛋白(或微管)头对尾稳态聚合的理论有所扩展。单体通量和ATP通量都可以用X和模型的速率常数来表示。当X趋于0(通过改变ATP、ADP和Pi的浓度)时,两种通量都趋于零;这个极限对应于ATP平衡。研究了速率常数对这些浓度的依赖性。讨论了单体动力学循环的自由能水平和自由能耗散率。推导了一种特殊情况下的稳态聚合物长度分布。