par Goormaghtigh, Erik ;De Meutter, J;Vanloo, Berlinda;Brasseur, Robert ;Rosseneu, Maryvonne;Ruysschaert, Jean Marie
Référence Biochimica et biophysica acta, 1006, 1, page (147-150)
Publication Publié, 1989-11
Référence Biochimica et biophysica acta, 1006, 1, page (147-150)
Publication Publié, 1989-11
Article révisé par les pairs
Résumé : | The secondary structure of the apo B-100 protein present in human low density lipoprotein has been investigated by transmission and attenuated total reflection infrared spectroscopy. The amount of beta-sheet (41%) is significantly higher than that determined by CD spectroscopy in the present study (12%) and elsewhere (15-16%). The high percentage of beta-sheet structure in apo B-100 supports the importance of such segments in maintaining the lipid-protein assembly in LDL. Polarized infrared spectroscopy indicates that the beta-sheet component of apo B-100 adopts a preferential orientation with respect to the phospholipid monolayer surrounding the LDL, whereas no such orientation is observed for the other secondary structure components. |