We used fluorescence and electronic absorption spectroscopy to study the molecular weight dependence of macromolecule-induced folding in a chain-centered meta-phenylene ethynylene (mPE) oligomer. Analogous to the ability of intrinsically unstructured proteins (IUPs) to induce folding of globular proteins in cellular environments, we show that macromolecules attached to both ends of an mPE dodecamer induce the foldamer to collapse into a presumed helical conformation. The collapse is especially prominent once the macromolecule segments become larger than ca. 50 kDa. For sufficiently large macromolecules, the conformational structuring occurs even in solvents that normally denature the foldamer. Based on these findings, chain-centered foldamers might find use as models to investigate the fundamental macromolecular physics of IUPs.