Abstract
The sequences of the human apo A-I and A-IV proteins contain respectively seven and eleven helical repeats of 17 residues, which were fully characterized. In discoidal lipid-apoprotein complexes, these helixes are oriented parallel to the phospholipid acyl chains around the edge of the disc, and antiparallel to each other. The residues on the side of the contiguous helixes are in close vicinity and can form salt bridges. Computer modeling of apo A-I- and apo A-IV-DPPC discoidal complexes, by energy minimisation procedures, suggests that electrostatic interactions between charged residues can significantly contribute to the stability of the apoprotein-lipid complexes.
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© 1993 Springer Science+Business Media Dordrecht
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Vanloo, B., De Pauw, M., Lins, L., Brasseur, R., Ruysschaert, JM., Rosseneu, M. (1993). Contribution of Helix-Helix Interactions to the Stability of Apolipoprotein-Lipid Complexes. In: Catapano, A.L., Gotto, A.M., Smith, L.C., Paoletti, R. (eds) Drugs Affecting Lipid Metabolism. Medical Science Symposia Series, vol 2. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-1703-6_7
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DOI: https://doi.org/10.1007/978-94-011-1703-6_7
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