The rate of crystal nucleation of colloids and globular proteins can be enhanced by critical density fluctuations. It has been argued that a closely related phenomenon influences the rate of intramolecular "crystallization" of single-chain polymers. We report Monte Carlo simulations of the free-energy barrier that separates the crystalline state of a homopolymer chain from the disordered state. The simulations show that the barrier for nucleation of the ordered state is drastically lowered as the disordered state changes from a coil to a globule. We discuss the relation of the present findings to intramolecular nucleation of heteropolymers, such as proteins.
J. Phys. Chem. B

Hu, W., & Frenkel, D. (2006). Effect of the coil-globule transition on the free-energy barrier for intrachain crystal nucleation. J. Phys. Chem. B, 110, 3734–3737. doi:10.1021/jp056679g