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Updated: Aug 5, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
[Bending fluctuations of the alpha-helix and the dynamics of enzyme-substrate interactions]
Abstract:
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.
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