The solution structure of a recombinant mutant [rSP-C (FFI)] of the human surfactant-associatedprotein C (hSP-C) in a mixture of chloroform andmethanol was determined by high-resolution NMR spectroscopy. rSP-C (FFI) contains a helix from Phe5 to theC-terminal Leu34 andis thus longer by two residues than the helix of porcine SP-C (pSP-C), which is reportedto start at Val7 in the same solvent. Two sets of resonances at the C-terminus of the peptide were observed, which are explained by low-order oligomerization, probably dimerization of rSP-C (FFI) in its a-helical form. .
