Open AccessStructure and orientation of the surfactant‐associated protein C in a lipid bilayer
Author(s) -
VANDENBUSSCHE Guy,
CLERCX Anne,
CURSTEDT Tore,
JOHANSSON Jan,
JÖRNVALL Hans,
RUYSSCHAERT JeanMarie
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb19848.x
Subject(s) - bilayer , lipid bilayer , pulmonary surfactant , protein secondary structure , dichroic glass , chemistry , crystallography , attenuated total reflection , infrared spectroscopy , fourier transform infrared spectroscopy , membrane , biophysics , materials science , biochemistry , organic chemistry , biology , optics , nanotechnology , physics
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 procine SP‐C adopt mainly an α‐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 α‐helical content. Dichroic measurements show that, in both cases, the long axis of the α‐helix is oriented parallel to the lipid acyl chains.