title: Evaluation of the secondary structure of apo B-100 in low-density lipoprotein (LDL) by infrared spectroscopy.
abstract: 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.
authors: Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
authors: E
authors: E
authors: Goormaghtigh
authors: J
authors: J
authors: De Meutter
authors: B
authors: B
authors: Vanloo
authors: R
authors: R
authors: Brasseur
authors: M
authors: M
authors: Rosseneu
authors: J M
authors: JM
authors: Ruysschaert
mesh_terms: D053299:Apolipoprotein B-100; D001055:Apolipoproteins B; D002942:Circular Dichroism; D005583:Fourier Analysis; D008077:Lipoproteins, LDL / Q000032:analysis*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
chemical_list: D053299:Apolipoprotein B-100; D001055:Apolipoproteins B; D008077:Lipoproteins, LDL