Size distribution of protein polymers

摘要: Abstract Theoretical analyses were made on the size distribution of tubular or helical polymers globular protein molecules in reversible polymerization. In true final equilibrium, polymerization approximates to a kind crystallization and average degree becomes very large; nevertheless, is simple exponential type, same as found macromolecular chemistry ( Flory, 1953 ). Even when spontaneous nucleation inhibited number given, must tend towards type. Free energy due deviation from equilibrium was calculated. It much smaller than main free coming monomer-polymer equilibrium. Kinetics showed that having characteristics usually consists three stages—nucleation, growth redistribution polymer size. first second stages where rate depolymerization negligible, concentration monomers approaches closely value. third stage, both take place nearly at rate, slowly transformed into The relaxation time for such estimated function constants under various conditions. All theoretical results are quantitatively good agreement with experimental data proteins actin flagellin. Brief added two-dimensional membraneous distorted polymers.