Number of the records: 1  

Equilibrium thermodynamics and the genesis of protein-protein complexes in cells

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    SYSNO ASEP0545775
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleEquilibrium thermodynamics and the genesis of protein-protein complexes in cells
    Author(s) Jennings, R.C. (IT)
    Belgio, Erica (MBU-M)
    Zucchelli, G. (IT)
    Source TitleRendiconti Lincei. Scienze Fisiche e Naturali. - : Springer - ISSN 2037-4631
    Roč. 32, č. 3 (2021), s. 417-426
    Number of pages10 s.
    Languageeng - English
    CountryIT - Italy
    KeywordsThermodynamics in biology ; Biological complexity ; Subcellular complexes ; Multi-protein complexes ; Thermodynamics second law
    Subject RIVEE - Microbiology, Virology
    OECD categoryMicrobiology
    R&D ProjectsGA19-11494S GA ČR - Czech Science Foundation (CSF)
    ED2.1.00/19.0392 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingOpen access
    Institutional supportMBU-M - RVO:61388971
    UT WOS000663505000001
    EID SCOPUS85108338565
    DOI10.1007/s12210-021-01004-1
    AnnotationIt is often thought that the structural complexity of living organisms places Life outside the laws of Physics. According to the Second Law of Thermodynamics, inanimate matter tends towards ever-increasing randomness. Most thermodynamic studies on the living system are course-grained in the sense that it is the whole organism which is considered and they lack microscopic details. In these studies, as the living system is an open system, non-linear thermodynamics have been used. This requires that a number of assumptions be made concerning the living system itself, which may not be correct in organisms living under natural environmental conditions. In the present study, we depart from this approach and use a fine-grained analysis of the genesis of subcellular protein complex structures. The analysis is performed in terms of classical equilibrium thermodynamics using the acquired knowledge of protein/protein interactions. In this way, it is demonstrated that the spontaneous creation of ordered subcellular structures occurs in accordance with the Second Law of Thermodynamics. We specifically consider the simple example of protein dimer and trimer formation from its monomer components, both in vitro and with chaperone assistance in vivo. The entropy decrease associated with protein complex assembly, on which the continuing debate is founded, is shown to be a relatively small component in the overall and positive entropy increase.
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2022
    Electronic addresshttps://link.springer.com/article/10.1007%2Fs12210-021-01004-1
Number of the records: 1  

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