Protein folding as a nonlinear nonequilibrium thermodynamic process.
Biofurcational theory of protein folding is developed describing the process of formation of protein native structure as a sequence of non-equilibrium irreversible fluctuations, specific for a particular protein. The model gives explanation to all characteristic features of the folding process: stochastic mechanism, short time and precision of proteins self-assembling. A constructive role of entropy in the formation of a highly ordered structure out of disorder is discussed. A numerical method of a priori calculations of polypeptide structures basing on principles of bifractional folding model is presented.
Popov
E M
EM
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
D019277:Entropy; D009842:Oligopeptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D009842:Oligopeptides; D011506:Proteins