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Raman spectroscopy was used to determine the conformation of the disulfide linkage between cysteine residues in the homodimeric construct of the N-terminal alpha helical domain of surfactant protein B (dSP-B 1–25 ). The conformation of the disulfide bond between cysteine residues in position 8 of the homodimer of dSP-B 1–25 was compared with that of a truncated homodimer (dSP-B ...