Violation of the fluctuation-dissipation theorem in a protein system
Violation of the fluctuation-dissipation theorem in a protein system
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DOI：
10.1529/biophysj.106.100487
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发表时间：
2007-08-01
影响因子：
3.4
通讯作者：
Takano, Mitsunori
中科院分区：
文献类型：
--
作者：
Hayashi, Kumiko;Takano, Mitsunori
我们报告的结果进行了弹性网络模型的蛋白质肌球蛋白的分子动力学模拟。淬灭系统，我们观察到的密度相关函数和密度响应函数，经常在结构玻璃和自旋玻璃研究的玻璃行为。在平衡状态下，波动-响应关系是波动-耗散定理的代表性关系，它认为密度相关函数与密度响应函数之比等于环境温度。然而，在我们所研究的猝灭系统中，这种关系是可以被破坏的。在该关系不成立的情况下，可以将该比率视为有效温度。我们发现肌球蛋白的有效温度高于环境温度。我们讨论了该有效温度与肌球蛋白分子中ATP水解后发生的能量转换之间的关系。
We report the results of molecular dynamics simulations of the protein myosin carried out with an elastic network model. Quenching the system, we observe glassy behavior of a density correlation function and a density response function that are often investigated in structure glasses and spin glasses. In the equilibrium, the fluctuation-response relation, a representative relation of the fluctuation-dissipation theorem, holds that the ratio of the density correlation function to the density response function is equal to the temperature of the environment. Weshow that, in the quenched system that we study, this relation can be violated. In the case that this relation does not hold, this ratio can be regarded as an effective temperature. We find that this effective temperature of myosin is higher than the temperature of the environment. We discuss the relation between this effective temperature and energy transduction that occurs after ATP hydrolysis in the myosin molecule.