The structural transformation in the coil-globule transition of a single flexible lattice chain has been investigated using dynamic Monte Carlo simulations. The results based upon ensemble averaging illustrated that for the homopolymers with Limited chain length; an intermediate state with a dense-core and molten-shell structure reversibly occurs in the transition region. It was attributed to a special microphase separation behavior in an isolated coil, performing with densifying the dense core and contracting the thin shell. The continuous appearance of the size transition and its tendency to discontinuity at the theta temperature with the chain length approaching infinity were illustrated by the coexistence curves of the monomers with limited chain length. A possible explanation and its implications to the general mechanism of protein folding are also discussed.