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Pulmonary surfactant contains less than 1 wt% of the very non-polar surfactant protein C (SP-C). In most animal species the major form of SP-C is a 35-residue peptide chain which contains two thioester-linked palmitoyl groups, giving a total molecular mass of 4.2 kDa. Several minor variants of SP-C exist, formed from N-terminal truncation, lysine palmitoylation, methionine oxidation and C-terminal esterification. The primary structure is evolutionarily conserved and SP-C appears to be the only constituent which is unique to pulmonary surfactant, indicating important and specific functions. The three-dimensional structure in an aqueous mixed organic solvent determined by NMR spectroscopy revealed one continuous 37 Å long α-helix encompassing residues 9–34 as the only regular structural element. The central 23 Å of the helix contains exclusively aliphatic residues with branched side-chains, mainly valines, and …