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 sequence derived from ferredoxin I, with a Pro-Asp two-residue type I turn which is uncommon in beta-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 beta-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.
Searle
M S
MS
Department of Chemistry, University Park, Nottingham, UK. mark.searle@nottingham.ac.uk
Jourdan
M
M
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D013499:Surface Properties
D008823:Micelles; D010455:Peptides