Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles

Biochim Biophys Acta. 1987 Jan 30;911(2):144-53. doi: 10.1016/0167-4838(87)90003-3.


delta-Haemolysin in mixed micelles with perdeuterated dodecylphosphocholine was investigated with two-dimensional proton nuclear magnetic resonance experiments at 500 MHz. A single set of resonance lines was observed for the micelle-bound polypeptide, indicating that delta-haemolysin adopts a single conformation in this environment. Nearly complete, sequence-specific assignments were obtained for the segment 5-23 of this 26-residue polypeptide chain. From the sequential connectivities and numerous medium-range nuclear Overhauser effects this central portion of the molecule was found to form an extended helix with pronounced amphipathic distribution of polar and nonpolar amino acid side-chains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Hemolysin Proteins*
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Micelles
  • Phosphorylcholine / analogs & derivatives
  • Protein Conformation


  • Bacterial Proteins
  • Hemolysin Proteins
  • Micelles
  • Phosphorylcholine
  • dodecylphosphocholine
  • delta hemolysin protein, Staphylococcus aureus