Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles.
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.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D010767:Phosphorylcholine / Q000031:analogs & derivatives; D011487:Protein Conformation
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D008823:Micelles; D010767:Phosphorylcholine; C028810:dodecylphosphocholine; C025994:delta hemolysin protein, Staphylococcus aureus