مفارقة البروتين السائر: لماذا يصل الأبعد أسرع؟ سريع

الملخص الأصلي

كما كتبه المؤلفون، بالإنجليزية arXiv:2607.27998v1

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.