Human Jagged‐1 is predicted to contain 16 epidermal growth factor‐like (EGF) repeats. The oxidative folding of EGF‐2, despite the several conditions tested, systematically led to complex mixtures. A longer peptide spanning the C‐terminal part of EGF‐1 and the complete EGF‐2 repeat, on the contrary, could be readily refolded. This peptide, which corresponds to the entire exon 6 of the Jagged‐1 gene, thus represents an autonomously folding unit. We show that it is structured in solution, as suggested by circular dichroism and NMR spectroscopy, and displays an EGF‐like disulfide bond topology, as determined by disulfide mapping.