Melittin bound to dodecylphosphocholine micelles. H-NMR assignments and global conformational features.
Assignments have been obtained for most of the H-NMR lines of melittin bound to fully deuterated dodecylphosphocholine micelles by combined use of two-dimensional spin echo correlated spectroscopy and one-dimensional NMR methods. Nuclear Overhauser enhancement measurements showed that the mobility of the entire polypeptide chain is reduced by binding of melittin to the detergent micelle and that the amino-terminal and carboxy-terminal halves of the primary structure constitute separate, compact domains within the conformation of micelle-bound melittin. p2H titration experiments showed that the presence of positive charges on the four amino groups of melittin had little influence on the conformation of the micelle-bound polypeptide. Titration of tetrameric melittin with detergent provided evidence that melittin assumes similar conformations as a self-aggregated tetramer and as a monomer bound to micelles.
D001514:Bee Venoms / Q000378:metabolism*; D002794:Choline / Q000031:analogs & derivatives*; D003102:Colloids; D009682:Magnetic Resonance Spectroscopy; D008555:Melitten / Q000378:metabolism*; D008823:Micelles; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000378:metabolism; D011487:Protein Conformation
D001514:Bee Venoms; D003102:Colloids; D008823:Micelles; D010767:Phosphorylcholine; D008555:Melitten; C028810:dodecylphosphocholine; D002794:Choline