Previous strategies of peptoid folding have focused on identifying single dominant interactions, whereas peptide research has shown that identifying multiple, weak, and cooperative interactions might be a better strategy to understand folding. Towards this goal, a few such interactions have been deciphered in this work, including intramolecular C–H⋯O/X weak hydrogen bonding interactions and N–H⋯N type hydrogen bonding. We also deciphered intermolecular C–X⋯O halogen bonding in the aromatic peptoid model systems. Both intramolecular and intermolecular weak interactions have been evaluated by X-ray crystallography and computational modeling. These interactions bias ω-dihedral angle in the trans configuration, as evaluated by NMR spectroscopy in the solution phase and the solid-state via X-ray crystallography. We established that fixing the ω-dihedral in the trans-amide configuration leads to the identification of the web of weak noncovalent interactions that are otherwise non-trivial to decipher. This new design strategy elucidates the control of peptoid amide isomerization that might be needed to access new secondary structures, facilitating the better mimicking of peptides.