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 kineti...
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| Format: | Article |
| Language: | English |
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Samara State Technical University
2013-12-01
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| Series: | Vestnik Samarskogo Gosudarstvennogo Tehničeskogo Universiteta. Seriâ: Fiziko-Matematičeskie Nauki |
| Subjects: | |
| Online Access: | https://journals.eco-vector.com/1991-8615/article/viewFile/34719/23070 |
| _version_ | 1818024582364266496 |
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| author | Vladik Avanesovich Avetisov Al'bert Khakimovich Bikulov Alexander Petrovich Zubarev |
| author_facet | Vladik Avanesovich Avetisov Al'bert Khakimovich Bikulov Alexander Petrovich Zubarev |
| author_sort | Vladik Avanesovich Avetisov |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-10T04:02:30Z |
| format | Article |
| id | doaj.art-7219fa862e5b426685ebba4b291d43e4 |
| institution | Directory Open Access Journal |
| issn | 1991-8615 2310-7081 |
| language | English |
| last_indexed | 2024-12-10T04:02:30Z |
| publishDate | 2013-12-01 |
| publisher | Samara State Technical University |
| record_format | Article |
| series | Vestnik Samarskogo Gosudarstvennogo Tehničeskogo Universiteta. Seriâ: Fiziko-Matematičeskie Nauki |
| spelling | doaj.art-7219fa862e5b426685ebba4b291d43e42022-12-22T02:02:57ZengSamara State Technical UniversityVestnik Samarskogo Gosudarstvennogo Tehničeskogo Universiteta. Seriâ: Fiziko-Matematičeskie Nauki1991-86152310-70812013-12-0117131532510.14498/vsgtu115431232Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobinVladik Avanesovich Avetisov0Al'bert Khakimovich Bikulov1Alexander Petrovich Zubarev2N. N. Semenov Institute of Chemical Physics, Russian Academy of SciencesN. N. Semenov Institute of Chemical Physics, Russian Academy of SciencesSamara State Transport UniversityIn 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.https://journals.eco-vector.com/1991-8615/article/viewFile/34719/23070co rebinding to myoglobinprotein dynamicsenzyme kineticsmathematical modelingultrametric random walk-adic numbers |
| spellingShingle | Vladik Avanesovich Avetisov Al'bert Khakimovich Bikulov Alexander Petrovich Zubarev Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin Vestnik Samarskogo Gosudarstvennogo Tehničeskogo Universiteta. Seriâ: Fiziko-Matematičeskie Nauki co rebinding to myoglobin protein dynamics enzyme kinetics mathematical modeling ultrametric random walk -adic numbers |
| title | Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin |
| title_full | Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin |
| title_fullStr | Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin |
| title_full_unstemmed | Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin |
| title_short | Ultrametricity as a basis for organization of protein molecules: CO binding to myoglobin |
| title_sort | ultrametricity as a basis for organization of protein molecules co binding to myoglobin |
| topic | co rebinding to myoglobin protein dynamics enzyme kinetics mathematical modeling ultrametric random walk -adic numbers |
| url | https://journals.eco-vector.com/1991-8615/article/viewFile/34719/23070 |
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