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Conformational Properties of Apolipoproteins Studied by Computer Graphics

  • J-L. De Coen
  • J-P. Kocher
  • C. Delcroix
  • J-F. Lontie
  • C. L. Malmendier
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 285)

Abstract

The physical properties of apolipoproteins in solution and when interacting with lipids have been extensively studied using various experimental methods ( 1 ) . In water, these molecules appear to be in equilibrium between a statistical coil and some folded conformers containing α-helices. When interacting with lipids, the α-helical content increases to reach values around 60% for apolipoprotein A-II for example. Taking these observations into account and looking at the results obtained when rules to predict secondary structure are applied to the sequence of apo A-II we proposed recently ( 2 ) that the tertiary structure of this molecule could be similar to the one of uteroglobin which is a little steroid binding protein of known crystalline structure ( 3 ). In particular, we observed that the regions of high helical content appear to be located at similar posi tions in the two molecules being in both cases delineated by proline residues. Furthermore, the occurrence of these helical regions gives rise for the two molecules to a clustering of hydrophobic residues. In the crystal, uteroglobin is a dimer made of two identical monomer units containing each four α-helices which are packed in space according to the scheme depicted on Fig. 1.

Keywords

Tertiary Structure Hydrophobic Surface Hydrophobic Residue Conformational Property Polar Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    H.J. Pownall, Q. Pao, D. Hickson, J.T. Sparrow, A.M. Gotto Jr. Thermodynamics of lipid-protein association in human plasma lipoproteins, Biophys. J., 37:175 (1982)PubMedCrossRefGoogle Scholar
  2. 2.
    J-L. De Coen, M. Deboeck, C. Delcroix, J-F. Lontie, C. L. Malmen dier, A proposed folding pattern for apolipoprotein A-II based on a structural analogy with uteroglobin, Proc. Natl. Acad. Sci. USA, 85:5669 (1988) .CrossRefGoogle Scholar
  3. 3.
    I. Morize, E. Surcouf, M.C. Vaney, Y. Epelboin, M. Fridlansky, F. Milgrom, J-P. Mornon, Refinement of the C2221 crystal form of oxidized uteroglobin at 1.34 A resolution, J. Mol. Biol. 194:725 (1987)PubMedCrossRefGoogle Scholar
  4. 4.
    P. Delhaise, M. Bardiaux, S. Wodak, Interactive computer animation of macromolecules, J. Mol. Graphics 2:103 (1984)CrossRefGoogle Scholar
  5. 5.
    F. Soetewey, M-J. Lievens, R. Vercaemst, M. Rosseneu, H. Peeters, V. Brown, Ionization behaviour of native apolipoproteins and their complexes with dimyristoyl lecithin, Eur. J. Biochem., 79:259 (1977)PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • J-L. De Coen
    • 1
  • J-P. Kocher
    • 1
  • C. Delcroix
    • 1
  • J-F. Lontie
    • 1
  • C. L. Malmendier
    • 1
  1. 1.Fondation de Recherche sur l’AtheroscleroseBrusselsBelgium

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