Templating peptide folding on the surface of a micelle: Nucleating the formation of a beta-hairpin

NMR spectroscopy is used to show that a 20-residue beta-hairpin peptide seq uence derived from ferredoxin I, with a Pro-Asp two-residue type I turn whi ch is uncommon in beta-hairpins, is unstructured in aqueous solution but sh ows NOE evidence for partial folding in the presence of sodium dodecylsulph ate micelles. The peptide has a number of lysine residues in the N-terminal beta-strand capable of interacting with the micelle surface and templating the partial folding of the hairpin by reducing the entropic cost of orderi ng the peptide backbone. (C) 2000 Published by Elsevier Science Ltd.