论文标题
蛋白质分子在功能态下的构象动力学的超级学理论，以及对CO与肌红蛋白结合的动力学的实验描述
Ultrametric theory of conformational dynamics of protein molecules in a functional state and the description of experiments on the kinetics of CO binding to myoglobin
论文作者
论文摘要
该论文致力于对蛋白质分子构象动力学理论的系统描述。作为该理论的应用的一个例子，我们提供了有关CO与肌红蛋白结合的动力学的完整分析描述，该实验是由30多年前的Frauenfelder组进行的，并获得了研究基础实验的状态，以研究蛋白质分子波动动力学的性能。早在2001年，作者就可以证明，在具有反应水槽的超级随机行走模型中，可以在高温度区域中复制CO与肌红蛋白的实验曲线。后来，在2010年，作者提出了一个修改模型，并基于其数值分析，证明该模型可以在实验中涵盖的整个温度范围内再现实验结果。在本研究中，基于先前提出的模型，我们制定了蛋白质分子构象动力学的严格数学理论。我们证明，提出的理论不仅提供了整个温度范围内（60 \ div300 \右）$ k的完整描述，在观察时间窗口中，在$ \ left的观察时间窗口（10^{ - 7} \ 7} \ div10^{2} {2} {2} {2} {2} \右）$ s $ s的统一性，并允许一个统一的蛋白质流动性，也可以实现蛋白质的统一。自相似的方式。迄今为止一直隐藏的蛋白质分子的这种特定特征显着扩展了蛋白质显然拥有的动态对称性思想。此外，我们表明该模型在$ \ left的低温范围内（60 \ div180 \ right）$ k在实验中未涵盖的低温范围（超过$ 10^{2} $ s），为实验动力学曲线的行为提供了预测。
The paper is devoted to a systematic account of the theory of conformational dynamics of protein molecules. As an example of application of this theory, we provide a complete analytical description of experiments on the kinetics of CO binding to myoglobin, which were carried out by the group of Frauenfelder more than 30 years ago and acquired the status of base experiments for studying the properties of the fluctuation dynamic mobility of protein molecules. As early as 2001, the authors could demonstrate that, within the model of ultrametric random walk with a reaction sink, the experimental curves of CO binding to myoglobin can be reproduced in the high-temperature region. Later, in 2010, the authors proposed a modified model and, based on its numerical analysis, demonstrated that this model can reproduces the experimental results over the whole temperature range covered in the experiment. In the present study, based on the previously proposed model, we formulate a rigorous mathematical theory of conformational dynamics of protein molecules. We demonstrate that the proposed theory provides not only a complete description of the experiment over the whole temperature range of $\left(60\div300\right)$ K and in the observation time window of $\left(10^{-7}\div10^{2}\right)$ s but also a unified picture of the conformational mobility of a protein molecule, as well as allows one to realize the fact that the mobility changes in a self-similar way. This specific feature of protein molecules, which has remained hidden to date, significantly expands the ideas of dynamic symmetry that proteins apparently possess. In addition, we show that the model provides a prediction for the behavior of the kinetic curves of the experiment in the low-temperature range of $\left(60\div180\right)$ K at times not covered by the experiment (more than $10^{2}$ s).
