Conformation of human apolipoprotein C-I in a lipid-mimetic environment determined by CD and NMR spectroscopy.

@article{Rozek1999ConformationOH,
  title={Conformation of human apolipoprotein C-I in a lipid-mimetic environment determined by CD and NMR spectroscopy.},
  author={Annett Rozek and James T. Sparrow and Karl H. Weisgraber and Robert J Cushley},
  journal={Biochemistry},
  year={1999},
  volume={38 44},
  pages={14475-84}
}
The high-resolution conformation of human apoC-I in complexes with sodium dodecyl sulfate (SDS) is presented. As estimated from CD data, apoC-I adopts 54% helical secondary structure when bound to SDS, which is similar to the helical content previously found with phospholipids. The NMR-derived conformation of apoC-I is composed of two amphipathic helices, residues 7-29 and 38-52, separated by a flexible linker. The N-terminal helix contains a mobile hinge involving residues 12-15. The… CONTINUE READING