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Monte carlo simulations of enzyme reactions in two dimensions: fractal kinetics and spatial segregation.

机译:在两个方面对酶反应进行蒙特卡洛模拟:分形动力学和空间分离。

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摘要

Conventional equations for enzyme kinetics are based on mass-action laws, that may fail in low-dimensional and disordered media such as biological membranes. We present Monte Carlo simulations of an isolated Michaelis-Menten enzyme reaction on two-dimensional lattices with varying obstacle densities, as models of biological membranes. The model predicts that, as a result of anomalous diffusion on these low-dimensional media, the kinetics are of the fractal type. Consequently, the conventional equations for enzyme kinetics fail to describe the reaction. In particular, we show that the quasi-stationary-state assumption can hardly be retained in these conditions. Moreover, the fractal characteristics of the kinetics are increasingly pronounced as obstacle density and initial substrate concentration increase. The simulations indicate that these two influences are mainly additive. Finally, the simulations show pronounced S-P segregation over the lattice at obstacle densities compatible with in vivo conditions. This phenomenon could be a source of spatial self organization in biological membranes.
机译:酶动力学的常规方程式基于质量作用定律,在低维和无序的介质(例如生物膜)中可能会失效。我们提出了具有不同障碍物密度的二维晶格上的孤立Michaelis-Menten酶反应的蒙特卡罗模拟,作为生物膜的模型。该模型预测,由于在这些低维介质上异常扩散的结果,动力学是分形的。因此,酶动力学的常规方程式无法描述该反应。特别是,我们证明了在这些条件下几乎不能保留准平稳状态假设。此外,随着障碍物密度和初始底物浓度的增加,动力学的分形特征越来越明显。仿真表明这两个影响主要是相加的。最后,模拟显示在与体内条件相容的障碍物密度下晶格上明显的S-P偏析。这种现象可能是生物膜中空间自我组织的来源。

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