Templating peptide folding on the surface of a micelle: nucleating the formation of a β-hairpin

NMR spectroscopy is used to show that a 20-residue β-hairpin peptide sequence derived from ferredoxin I, with a Pro-Asp two-residue type I turn which is uncommon in β-hairpins, is unstructured in aqueous solution but shows NOE evidence for partial folding in the presence of sodium dodecylsulphate micelles. The peptide has a number of lysine residues in the N-terminal β-strand capable of interacting with the micelle surface and templating the partial folding of the hairpin by reducing the entropic cost of ordering the peptide backbone.