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Structure and orientation of the surfactant-associated protein C in a lipid bilayer.

par Vandenbussche, Guy ;Clercx, Anne ;Curstedt, T;Johansson, J;Jornvall, H.;Ruysschaert, Jean Marie
Référence European journal of biochemistry / FEBS, 203, 1-2, page (201-209)
Publication Publié, 1992-01

Article révisé par les pairs

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Résumé :

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.