We propose a heteropolymer design scheme, to tune monomer distributions that stabilize or destabilize the collapsed globular conformation relative to random sequencing. Polymer sequences trained via globular templating are mapped to a one-dimensional Ising-like model, and inverse Monte Carlo simulations are performed to determine an-effective interaction, between monomers that reproduces intrasequence correlations. Heteropolymer sequences generated using this effective interaction quantitatively reproduce the coil-to-globule transition with increasing polymer hydrophobicity observed for templated sequences. Through potential scaling, the range of transition hydrophobic fractions required to collapse the polymer opens up by a factor of 2, from a minimum fraction of 17% to a maximum of 32% for the longest polymers simulated. Collapsed conformations are favored by sequences in which there is intermediate segregation of hydrophobic and hydrophilic units along the backbone, while monomer integration favors coils.