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Biochim Biophys Acta. 1987 Jan 30;911(2):144-53.

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.

[Indexed for MEDLINE]

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