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Structure function relationship of the plasma apolipoproteins: a computational approach based on hydrophobicity
1Department Clinical Biochemistry, AZ St-Jan, Brugge, Belgium.
Annales De Biologie Clinique
|January 1, 1988
Abstract:
Using different hydrophobicity analysis techniques we investigated the structure-function relationship of the different apolipoproteins. Lipid-binding domains were localized and within this class of protein domains, lecithin-cholesterol acyltransferase activating and non-activating amphipathic helices could be differentiated. A hydrophobic moment analysis of the apolipoprotein E sequence yielded interesting data concerning its receptor-binding and heparin binding characteristics. Finally we discuss the amphiphilic helical characteristics of certain domains of the apolipoprotein B sequence.