Geodesic
Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin
Journal of Samara State Technical University, Ser. Physical and Mathematical Sciences, no. 1 (2013), pp. 315-325

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In this paper, the basic notions of ultrametric ($p$-adic) description of protein conformational dynamics and CO rebinding to myoglobin are presented. It is shown that one and the same model of the reaction — ultrametric diffusion type describes essentially different features of the rebinding kinetics at high-temperatures ($300{\div}200$ K) and low-temperatures ($180{\div}60$ K). We suggest this result indicates a special structural order in a protein molecule. Besides all the other structural features, it is organized by such a way that its conformational mobility changes self-similar from room temperature up to the cryogenic temperatures.
Keywords: CO rebinding to myoglobin, protein dynamics, enzyme kinetics, mathematical modeling, ultrametric random walk, $p$-adic numbers. 
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     title = {Ultrametricity as a basis for organization of protein molecules: {CO} binding to myoglobin},
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V. A. Avetisov; A. Kh. Bikulov; A. P. Zubarev. Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin. Journal of Samara State Technical University, Ser. Physical and Mathematical Sciences, no. 1 (2013), pp. 315-325. http://geodesic.mathdoc.fr/item/VSGTU_2013_1_a31/