Abstract
The conformation of a polymer in a solvent is typically defined by the solvent quality, which is a consequence of the solvent and macromolecule's chemistry. Yet, additional factors can affect the polymer conformation, such as non-covalent interactions to surfaces or other macromolecules, affecting the amount of polymer-solvent interactions. Herein, chemically folded polymers with protein-like architectures are studied and compared to their unfolded linear precursor in good solvents using rheology measurements. The current research reveals that permanent folding by intramolecular chemical cross-linking limits the chain mobility and therefore causes a reduction in polymer-solvent interactions, making a good solvent become theta. This change not only affects the "solvent quality" but also leads to a change in particle-particle interactions as a function of concentration. These findings provide crucial insight into the effects of intramolecular cross-links on macromolecule solubility and self-assembly, which are critical for mimicking structurally similar biological materials.
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