What NMR can tell us about where lung surfactant proteins live.
2H-NMR is beginning to provide some insights into the way in which the hydrophobic surfactant proteins SP-B and SP-C interact with phospholipid bilayers in multilamellar structures. Both proteins have a significant effect on slow bilayer motions. In many ways, the effect of SP-C on the surrounding bilayer is similar to that of other transmembrane proteins. Ca2+ appears to modify the way in which SP-C perturbs the bilayers containing DPPG. The effect of SP-B on bilayers differs, in subtle ways, from that expected for a transmembrane protein.
Morrow
M R
MR
Department of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Canada.
Taneva
S
S
Dico
A S
AS
Hancock
J
J
Keough
K M
KM
D015060:1,2-Dipalmitoylphosphatidylcholine; D000818:Animals; D003903:Deuterium; D006801:Humans; D008051:Lipid Bilayers; D008168:Lung / Q000737:chemistry / Q000502:physiology*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010715:Phosphatidylglycerols; D011510:Proteolipids / Q000737:chemistry*; D011663:Pulmonary Surfactants / Q000737:chemistry*
D008051:Lipid Bilayers; D010715:Phosphatidylglycerols; D011510:Proteolipids; D011663:Pulmonary Surfactants; D015060:1,2-Dipalmitoylphosphatidylcholine; D003903:Deuterium; C030345:1,2-dipalmitoylphosphatidylglycerol