High-resolution 1H NMR study of the solution structure of alamethicin.
A 1H NMR study of the peptide alamethicin, which forms voltage-gated ion channels in membranes, is described. The molecule was studied in methanol as a function of temperature and pH. A complete assignment of the spectra is given, including several stereospecific assignments. Alamethicin was found to have a structure substantially similar to the crystal although, in solution, the C-terminal dipeptide adopts a somewhat extended conformation. The overall conformation was insensitive to the ionization of the side chain of the only ionizable group, Glu-18.
D000408:Alamethicin; D000900:Anti-Bacterial Agents; D006859:Hydrogen; D007473:Ion Channels / Q000502:physiology; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008954:Models, Biological; D011487:Protein Conformation; D012996:Solutions
D000900:Anti-Bacterial Agents; D007473:Ion Channels; D012996:Solutions; D000408:Alamethicin; D006859:Hydrogen