Abstract
Experiments show that drying of the same protein colloidal solution in open (air) and closed systems results in two thermodynamically nonequilibrium processes differing in character of energy relaxation. It has been shown that fast removal of the water (evaporation in this case) from the protein-water system is crucial for the protein to stay in the nonequilibrium state. To a certain extent, this fact can be considered as a simplified experimental equivalent of fast adenosine triphosphoric acid (ATF) hydrolysis, a reaction common to living organisms, since fast removal of the water from the water-protein system is also typical of this reaction. This analogy, as well as the similarity (in appearance and types and scales of symmetry) of the protein structures resulting upon drying the protein colloidal solution in vitro and in vivo, suggests that the relaxation processes taking place at nonequilibrium protein self-organization are similar in thermodynamic parameters in both cases. Thus, there appears the possibility of studying the protein in both the equilibrium and nonequilibrium (as yet poorly understood) state.
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Translated from Zhurnal Tekhnichesko\(\overset{\lower0.5em\hbox{$\smash{\scriptscriptstyle\smile}$}}{l} \) Fiziki, Vol. 75, No. 9, 2005, pp. 129–131.
Original Russian Text Copyright © 2005 by Rapis.
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Rapis, E. Relaxation of the energy of the protein colloidal solution arising at drying in open and closed systems. Tech. Phys. 50, 1236–1238 (2005). https://doi.org/10.1134/1.2051470
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DOI: https://doi.org/10.1134/1.2051470