The rapid collapse of a linear homopolymer after abrupt fall in temperature or deterioration of the quality of the solvent leads to the advent of a folded non-equilibrium globule. The length of the chain in it is a fractal with the dimension μ ≤ 2 on small and μ = 3 on large scales. This is ensured by the non-self-intersection of the chain and the resulting spatial segregation from each other on all itself. Further relaxation of the folded globule occurs very slowly, only through reptation (diffusion crawling) of the chain along itself and leads to knotting of the polymer. The model of the folded globule makes it possible to explain from a consistent standpoint a whole number of properties of globular proteins. Predictions, the verification of which in the real or computer experiment should demonstrate the adequacy of our results, are formulated.
|Original language||English (US)|
|Number of pages||8|
|State||Published - 1988|
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