The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function.

  title={The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function.},
  author={Jere P. Segrest and Martin K. Jones and H de Loof and Christie G. Brouillette and Y. V. Venkatachalapathi and Gattadahalli M. Anantharamaiah},
  journal={Journal of lipid research},
  volume={33 2},
Site-directed mutagenesis and other molecular biology-based techniques are now available for probing the amphipathic alpha helix structural motif in the exchangeable apolipoproteins. Here we survey the published literature on lipid-binding and functional domains in apolipoproteins A-I, A-II, A-IV, C-I, C-II, C-III, and E and compare these results with recently developed computer methods for analysis of the location and properties of amphipathic helixes. This comparison suggests that there are… CONTINUE READING
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