The secondary structure of human very low density lipoproteins (VLDL)
has been quantitatively examined by using Fourier transform infrared (
FTIR) spectroscopy. Derivative spectroscopy was combined with band cur
ve-fitting procedures to quantitate the spectral information from the
amide I' band. Nine component bands were found under the broad amide I
' band which reflect the presence of various substructures. The second
ary structure is estimated to be 23% alpha-helix, 30% beta-sheets, 5%
turns, 29% unordered and 13% beta-strand or extended, not forming beta
-sheets, in contact with the lipid moiety. Comparison of the VLDL spec
trum with that of its lipid fraction, together with H-D exchange measu
rements, reveal strong protein-lipid interaction in agreement with pro
teolysis studies.