Understanding protein beta structures has been hindered by the challenge of designing small, well‐folded β‐sheet systems. A β‐capping motif was previously designed to help solve this problem, but not without limitations, as the termini of this β‐cap were not fully available for chain extension. Combining Coulombic side chain attractions with a Trp/Trp edge‐to‐face interaction we produced a new capping motif that provided greater β‐sheet stability. This stability was maintained even in systems lacking a turn locus with a high propensity for chain direction reversal. The Coulombic cap was shown to improve β‐sheet stability in a number of difficult systems, hence providing an additional tool for protein structure and folding studies.