Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin

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.