Although β‐hairpins are widespread in proteins, there is no tool to coax any small peptide to adopt a β‐hairpin conformation, regardless of sequence. Here, we report that δ‐linked γ(R)‐methyl‐ornithine (δMeOrn) provides an improved β‐turn template for inducing a β‐hairpin conformation in peptides. We developed a synthesis of protected δMeOrn as a building block suitable for use in Fmoc‐based solid‐phase peptide synthesis. The synthesis begins with l‐leucine and affords gram quantities of the Nα‐Boc‐Nδ‐Fmoc‐γ(R)‐methyl‐ornithine building block. X‐ray crystallography confirms that the δMeOrn turn unit adopts a folded structure in a macrocyclic β‐hairpin peptide. CD and NMR spectroscopy allow comparison of the δMeOrn turn template to the δ‐linked ornithine (δOrn) turn template that we previously introduced and to the popular d‐Pro‐Gly turn template. These studies show that the folding of the δMeOrn turn template is substantially better than that of δOrn and is comparable to d‐Pro‐Gly.