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.