Additional intra-and intermolecular interactions permit even greater structural control. Further, concentration effects exist since below a characteristic concentration, the entropic cost of chain collapse and chain-chain repulsion is greater than the benefit of avoiding contact with water. This extensive theoretical knowledge about protein folding along with significant information in the Protein Data Bank (PDB) paved the path for AlphaFold, an artificial intelligence (AI) platform that provides protein structural predictions given only the corresponding amino acid sequence. While this landmark advancement has significantly closed the gap in our ability to predict how protein sequence organization impacts its ultimate morphology, these advancements beg the question -is it possible to bridge the gap between design features and structural attributes for synthetic macromolecules which lack the precise organization of globular proteins?