Structure and orientation of the surfactant-associated protein C in a lipid bilayer.
The secondary structure of native and depalmitoylated porcine surfactant-associated protein C (SP-C) was studied by attenuated total reflection Fourier-transform infrared spectroscopy. Both forms of porcine SP-C adopt mainly an alpha-helical conformation. These two forms of the protein were reconstituted in a lipid bilayer. The insertion of the protein in a membrane is associated with an increase of the alpha-helical content. Dichroic measurements show that, in both cases, the long axis of the alpha-helix is oriented parallel to the lipid acyl chains.
Vandenbussche
G
G
Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
Clercx
A
A
Curstedt
T
T
Johansson
J
J
Jörnvall
H
H
Ruysschaert
J M
JM
D000818:Animals; D005583:Fourier Analysis; D008051:Lipid Bilayers; D011487:Protein Conformation; D011510:Proteolipids / Q000378:metabolism*; D011663:Pulmonary Surfactants / Q000378:metabolism*; D013055:Spectrophotometry, Infrared; D013552:Swine
D008051:Lipid Bilayers; D011510:Proteolipids; D011663:Pulmonary Surfactants