Synthesis, secondary structure and folding of the bend region of lung surfactant protein B.

Abstract excerpt

Previous theoretical analysis of the primary structure of lung surfactant protein SP-B indicates a disulfide-linked, hydrophobic midsequence that forms a hairpin-like motif. Here, we experimentally investigate the secondary structure of the disulfide-stabilized bend region by synthesizing two 12-residue analogs of the SP-B midsequence. The native peptide has the same sequence for residues 35 to 46 as native human...

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