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Equilibrium thermodynamics and the genesis of protein-protein complexes in cells
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SYSNO ASEP 0545775 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Equilibrium thermodynamics and the genesis of protein-protein complexes in cells Author(s) Jennings, R.C. (IT)
Belgio, Erica (MBU-M)
Zucchelli, G. (IT)Source Title Rendiconti Lincei. Scienze Fisiche e Naturali. - : Springer - ISSN 2037-4631
Roč. 32, č. 3 (2021), s. 417-426Number of pages 10 s. Language eng - English Country IT - Italy Keywords Thermodynamics in biology ; Biological complexity ; Subcellular complexes ; Multi-protein complexes ; Thermodynamics second law Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GA19-11494S GA ČR - Czech Science Foundation (CSF) ED2.1.00/19.0392 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000663505000001 EID SCOPUS 85108338565 DOI 10.1007/s12210-021-01004-1 Annotation It 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2022 Electronic address https://link.springer.com/article/10.1007%2Fs12210-021-01004-1
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