Abstract
A new nonequilibrium allotropic protein modification (for brevity, hereafter called a protos) obtained by in vitro self-assembly of cluster protein films and identified with in vivo protein folding has been experimentally observed and described in detail [1–7]. In vitro visualization of the dynamics of protein condensation in an open protein-water system under the nonequilibrium conditions (at a relatively fast water evaporation) both on the micro-and macrolevels provided the establishment of the chaotic nonlinear dynamics of the process. The protein film has no long-range order and is characterized by a morphologically new highly structurized order at the nano-and macrolevels. A number of new structural, electric, and magnetic properties of a protein considerably different from the properties observed for crystalline proteins formed under the equilibrium conditions have been established.
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Translated from Zhurnal Tekhnichesko\(\overset{\lower0.5em\hbox{$\smash{\scriptscriptstyle\smile}$}}{l} \) Fiziki, Vol. 70, No. 1, 2000, pp. 122–133.
Original Russian Text Copyright © 2000 by Rapis.
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Rapis, E.G. Self-assembly of cluster protein films (allotropic nonequilibrium noncrystalline modification) during the process or their condensation. Tech. Phys. 45, 121–131 (2000). https://doi.org/10.1134/1.1259582
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DOI: https://doi.org/10.1134/1.1259582