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.

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Вестн. Сам. гос. техн. ун-та. Сер. Физ.-мат. науки. 2013. 1 (30). С. 315-325 УДК 517.958:57 УЛЬТРАМЕТРИКА КАК ПРИНЦИП ОРГАНИЗАЦИИ БЕЛКОВЫХ МОЛЕКУЛ: КИНЕТИКА СВЯЗЫВАНИЯ СО МИОГЛОБИНОМ В. А. Аветисов1 , А. Х. Бикулов1 , А. П. Зубарев2 1 Институт химической физики им. Н. Н. Семенова РАН, Россия, 119991, Москва, ул. Косыгина, 4 2 Самарский государственный университет путей сообщения, Россия, 443066, Самара, 1-й Безымянный пер., 18. E-mails: vladik.avetisov@gmail.com, bikulov1903@rambler.ru, apzubarev@mail.ru Изложены основные идеи ультраметрического (p-адического) описания конфор- мационной динамики белковой молекулы и кинетики связывания СО миогло- бином. Показано, что существенно различные свойства кинетики связывания в высокотемпературной (300

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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