Nonequilibrium state of self-organized protein nanostructures

Early experiments (1988–2004) on drying out an open (far from equilibrium) colloid protein-water system in vitro at a sufficiently high rate of water evaporation allowed us to reveal for the first time the nonequilibrium state of protein during its self-organization. Thus, an experimental model of protein in vitro, which is to some extent reminiscent of its behavior in vivo, is realized. Based on these findings, we discuss the role of the nonequilibrium liquid-crystal state of protein at its self-organization in the living organism. The emphasis is on the information content of protein and phase transitions in it, as well as on the properties of the aqueous adenosine triphosphate(ATP)-adenosine diphosphate (ADP) system with regard to the rate of water removal. A hypothesis is put forward that the ATP-ADP system serves to accomplish a special mechanism of vital importance providing cyclic self-organization of protein in the high-energy state. It is hoped that an in-depth study of this state will form the basis for further advances in the science of protein not only in the equilibrium state (on the angstrom scale) but also in the nonequilibrium state from the nano-to macroscale.