Email this article Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin
- Authors: Avetisov V.A.1, Bikulov A.K.1, Zubarev A.P.2
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Affiliations:
- N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences
- Samara State Transport University
- Issue: Vol 17, No 1 (2013)
- Pages: 315-325
- Section: Articles
- URL: https://journal-vniispk.ru/1991-8615/article/view/34719
- DOI: https://doi.org/10.14498/vsgtu1154
- ID: 34719
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Abstract
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.
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##article.viewOnOriginalSite##About the authors
Vladik Avanesovich Avetisov
N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences
Email: avetisov@chph.ras.ru
Doctor of physico-mathematical sciences, Professor
Al'bert Khakimovich Bikulov
N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences
Email: bikulov1903@rambler.ru, beecul@mail.ru
Candidate of physico-mathematical sciences
Alexander Petrovich Zubarev
Samara State Transport University
Email: apzubarev@mail.ru
Candidate of physico-mathematical sciences, Associate professor
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