NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles
Peptaibol antiamoebin I: spatial structure, backbone dynamics, interaction with bicelles and lipid-protein nanodiscs, and pore formation in context of barrel-stave model.
ANTIAMOEBIN I IS LINEAR PEPTIDE, A MEMBER OF THE PEPTAIBOL FAMILY OF MEMBRANE CHANNEL FORMING PEPTIDES. HERE, ANTIAMOEBIN I IS REPRESENTED BY THE SEQUENCE (SEQRES)
ANTIAMOEBIN I IS A HEXADECAMERIC HELICAL PEPTIDE. THE N-TERM IS ACETYLATED (RESIDUE 0)
120 mM DHPC, 30 mM DMPC, 7.5 mM acetic acid, 2.5 mM sodium acetate, 1 mM [U-100% 13C; U-100% 15N] ANTIAMOEBIN I, 90% H2O/10% D2O