Interaction of apoprotein from porcine high-density lipoprotein with dimyristoyl lecithin. 1. The structure of the complexes.
The morphology and structural organisation of the complexes formed from the apoprotein of porcine high-density lipoprotein and dimyristoyl phosphatidylcholine (lecithin) have been studied using the technique of small-angle X-ray scattering. Scattering measurements made in solvents of varying electron density were interpreted in terms of a scattering-equivalent model for the structure of the complex. This model is described by an oblate ellipsoidal morphology with dimensions at 20 degrees C: major axis 11.0 nm, minor axis 5.5 nm. Within this overall shape the lipid hydrocarbon chains are organised in an apolar core whilst the lipid polar head groups and protein are located in a outer shell 0.85 nm in thickness. The oblate morphology demonstrates that the structure of the complex is directed by the fundamental bilayer organisation of the lecithin. The dimension of the minor axis (5.5 nm) indicates that phospholipid hydrocarbon chains are orientated perpendicular to the interface.
D000818:Animals; D001059:Apoproteins / Q000097:blood; D001665:Binding Sites; D008075:Lipoproteins, HDL / Q000097:blood; D009227:Myristic Acids; D010713:Phosphatidylcholines; D011485:Protein Binding; D011487:Protein Conformation; D013552:Swine; D014961:X-Ray Diffraction
D001059:Apoproteins; D008075:Lipoproteins, HDL; D009227:Myristic Acids; D010713:Phosphatidylcholines