Solid-state 15N-NMR evidence that gramicidin A can adopt two different backbone conformations in dimyristoylphosphatidylcholine model membrane preparations.
Using [15N-Val7]gramicidin A it is shown by solid state 15N-NMR that in dimyristoylphosphatidylcholine model membrane preparations evidence is obtained for two different backbone conformations of gramicidin. One of these conformations is the familiar channel state while a second conformation possesses very different dynamic and structural characteristics. The relative amounts of the conformations depend upon the solvent used to initially codissolve peptide and lipid. Furthermore, by incubation of the samples at modestly elevated temperatures a conversion can be induced from the non-channel to the channel state in a lipid environment.
Killian
J A
JA
Department of Chemistry, Florida State University, Tallahassee.
Nicholson
L K
LK
Cross
T A
TA
D002942:Circular Dichroism; D004134:Dimyristoylphosphatidylcholine; D006096:Gramicidin; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013696:Temperature
D008051:Lipid Bilayers; D006096:Gramicidin; D004134:Dimyristoylphosphatidylcholine