驱动蛋白分子马达的化学力学模型中的姆佩姆巴效应
Mpemba effect in a chemomechanical model of the Kinesin molecular motor
浏览论文内容
中文总结 AI 辅助
该研究证实驱动蛋白分子马达的六态化学力学模型中存在姆佩姆巴效应，发现马达速度弛豫反映其随机动力学的反常弛豫，为研究生物体内反常弛豫提供了新的基线与框架。
中文摘要 AI 辅助
姆佩姆巴效应指的是，一个初始远离平衡态的系统比初始更接近平衡态的系统弛豫得更快，该效应已在广泛的物理系统中得到深入研究。相比之下，其在生物相关非平衡过程中的作用仍大多未被探索。本文研究了驱动蛋白分子马达的六态化学力学网络模型在平衡态和非平衡态下的反常弛豫。我们首先证实化学平衡中存在姆佩姆巴效应，并表明其许多定性特征可从基础自由能景观中得到理解。随后我们考察了力学和化学驱动的影响，结果显示，细致平衡的破缺主要重塑了姆佩姆巴相图，且在物理相关参数范围内未在定性上改变弛豫现象学。最后，我们证明马达速度的弛豫也反映了基础随机动力学的反常弛豫，从而确定了姆佩姆巴效应的一个实验可观测特征。我们的结果确立了分子马达作为研究生物体内反常弛豫的有前景基线，并为探索非平衡生化网络中的姆佩姆巴效应提供了更广泛的框架。
英文摘要
The Mpemba effect, wherein a system prepared farther from equilibrium relaxes faster than one initially closer to equilibrium, has been extensively investigated in a wide range of physical systems. In contrast, its role in biologically relevant non-equilibrium processes remains largely unexplored. Here, we investigate anomalous relaxation in the six-state chemomechanical network model of the Kinesin molecular motor under both equilibrium and non-equilibrium conditions. We first establish the existence of the Mpemba effect in chemical equilibrium and show that many of its qualitative features can be understood from the underlying free-energy landscape. We then examine the effects of mechanical and chemical driving, showing that breaking detailed balance primarily reshapes the Mpemba phase diagram without qualitatively altering the relaxation phenomenology over the physically relevant parameter regime. Finally, we demonstrate that the relaxation of the motor velocity also mirrors the anomalous relaxation of the underlying stochastic dynamics, thereby identifying an experimentally accessible signature of the Mpemba effect. Our results establish molecular motors as a promising baseline for studying anomalous relaxation in living systems and suggest a broader framework for exploring the Mpemba effect in non-equilibrium biochemical networks.
