Shaĭtan K V, Rubin A B
Mol Biol (Mosk). 1983 Nov-Dec;17(6):1280-96.
A stochastic model is developed for the dynamic behavior of proteins containing relatively rigid structural components. The paper considers the fluctuations of a gap between the rigid components and the dynamics of substrate--gap interactions associated with the formation of the enzyme-substrate complex. Electron-conformation interactions in the physical situation being considered are described by a model involving multiple diffusion movements within the configurational space having an absorption area. It has been shown that the limiting stage of catalysis (tau approximately 10(-2)-10(-4) s) is a specific structural configuration of the active center groups and substrate, formed during conformational motions, through which effective multi-center chemical interactions are made possible.
针对含有相对刚性结构成分的蛋白质的动态行为，建立了一个随机模型。本文考虑了刚性成分之间间隙的波动以及与酶 - 底物复合物形成相关的底物 - 间隙相互作用的动力学。在所考虑的物理情形中，电子 - 构象相互作用通过一个涉及在具有吸收区域的构型空间内多次扩散运动的模型来描述。结果表明，催化的极限阶段（τ约为10^(-2)-10^(-4)秒）是在构象运动过程中形成的活性中心基团和底物的特定结构构型，通过该构型使得有效的多中心化学相互作用成为可能。
