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A fractional calculus approach to self-similar protein dynamics.

机译:用于自相似蛋白质动力学的分数演算方法。

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摘要

Relaxation processes and reaction kinetics of proteins deviate from exponential behavior because of their large amount of conformational substrates. The dynamics are governed by many time scales and, therefore, the decay of the relaxation function or reactant concentration is slower than exponential. Applying the idea of self-similar dynamics, we derive a fractal scaling model that results in an equation in which the time derivative is replaced by a differentiation (d/dt)beta of non-integer order beta. The fractional order differential equation is solved by a Mittag-Leffler function. It depends on two parameters, a fundamental time scale tau 0 and a fractional order beta that can be interpreted as a self-similarity dimension of the dynamics. Application of the fractal model to ligand rebinding and pressure release measurements of myoglobin is demonstrated, and the connection of the model to considerations of energy barrier height distributions is shown.
机译:蛋白质的松弛过程和反应动力学因其大量的构象底物而偏离指数行为。动力学受许多时间尺度控制,因此,弛豫函数或反应物浓度的衰减比指数慢。应用自相似动力学的思想,我们得到了一个分形缩放模型,该模型产生了一个方程,其中时间导数被非整数阶β的微分(d / dt)β代替。分数阶微分方程由Mittag-Leffler函数求解。它取决于两个参数,基本时间标度tau 0和分数阶beta,可以将其解释为动力学的自相似维。证明了分形模型在肌红蛋白配体结合和压力释放测量中的应用,并显示了该模型与考虑能垒高度分布的联系。

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