[Bending fluctuations of the alpha-helix and the dynamics of enzyme-substrate interactions].
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.
D002268:Carboxypeptidases / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D013379:Substrate Specificity
D004798:Enzymes; D002268:Carboxypeptidases; D002918:Chymotrypsin
Izgibnye fluktuatsii alpha-spiraleĭ i dinamika ferment-substratnykh vzaimodeĭstviĭ.