Open AccessInvestigation of the membrane‐active peptides melittin and glucagon by photochemically induced dynamic‐nuclear‐polarization (photo‐CIDNP) NMR
Author(s) -
MAURER Till,
LÜCKE Christian,
RÜTERJANS Heinz
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb15796.x
Subject(s) - cidnp , melittin , chemistry , polarization (electrochemistry) , nuclear magnetic resonance , membrane , biochemistry , physics
The photochemically induced dynamic‐nuclear‐polarization (photo‐CIDNP) NMR technique was used to investigate the membrane‐active peptides melittin and glucagon. The experiments were performed both in the absence and presence of phospholipid vesicles in order to study the topography of the membrane‐bound state. From the results it can be concluded that the melittin peptide chain is oriented in such a way that the single tryptophan residue (Trp19) reaches into the membrane. In the case of glucagon, a binding interaction with vesicle membranes is indicated within the pH range 2–10, whereby the single tryptophan residue (Trp25) is buried in the lipid bilayer and the tyrosine and histidine residues are exposed to the aqueous solvent.