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