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The pulmonary surfactant prevents alveolar collapse and is required for normal pulmonary function. One of the important components of the surfactant besides phospholipids is surfactant‐associated protein C (SP‐C). SP‐C shows complex oligomerization behavior and a transition to β‐amyloid‐like fibril structures, which are not yet fully understood. Besides this nonspecific oligomerization, MS and chemical cross‐linking data combined with CD spectra provide evidence of a specific, mainly α‐helical, dimer at low to neutral pH. Furthermore, resistance to CNBr cleavage and dual NMR resonances of porcine and human recombinant SP‐C with Met32 replaced by isoleucine point to a dimerization site located at the C‐terminus of the hydrophobic α‐helix of SP‐C, where a strictly conserved heptapeptide sequence is found. Computational docking of two SP‐C helices, described here, reveals a dimer with a helix–helix …