Ultrametric random walk and dynamics of protein molecules

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The authors study the \(p\)-adic equations of an ultrametric random walk and its application to conformational dynamics of protein molecules. Two main experiments are proposed to determine the properties of mobility of protein molecules at temperatures from 300 to 4 K: the kinetics of CO binding to myoglobin and the spectral diffusion in proteins. It is found that the \(p\)-adic random walk allows to build a unified picture of the conformational mobility of protein molecules at low temperatures and that the mobility varies in a self-similar way.




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