Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayers.
Cytochrome b5 was reconstituted with a highly deuterated phospholipid to form ordered multilayers consisting of repeated centrosymmetric pairs of asymmetric lipid-protein bilayers. Lamellar neutron diffraction data were collected to approximately 29 A resolution, and have been interpreted using models for the interaction of the membrane-binding domain of cytochrome b5 with the lipid bilayer. A range of different models was examined, and those in which the protein penetrates well into the bilayer, possibly spanning it, are favored.
D000818:Animals; D002417:Cattle; D003573:Cytochrome b Group / Q000378:metabolism*; D015786:Cytochromes b5; D003903:Deuterium; D008051:Lipid Bilayers; D008099:Liver / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008968:Molecular Conformation; D011487:Protein Conformation; D013499:Surface Properties
D003573:Cytochrome b Group; D008051:Lipid Bilayers; D015786:Cytochromes b5; D003903:Deuterium