Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism.
The primary and secondary structure of human plasma apolipoprotein A-I and apolipoprotein E-3 have been analyzed to further our understanding of the secondary and tertiary conformation of these proteins and the structure and function of plasma lipoprotein particles. The methods used to analyze the primary sequence of these proteins used computer programs: (a) to identify repeated patterns within these proteins on the basis of conservative substitutions and similarities within the physicochemical properties of each residue; (b) for local averaging, hydrophobic moment, and Fourier analysis of the physicochemical properties; and (c) for secondary structure prediction of each protein carried out using homology, statistical, and information theory based methods. Circular dichroism was used to study purified lipid-protein complexes of each protein and quantitate the secondary structure in a lipid environment. The data from these analyses were integrated into a single secondary structure prediction to derive a model of each protein. The sequence homology within apolipoproteins A-I, E-3, and A-IV is used to derive a consensus sequence for two 11 amino acid repeating sequences in this family of proteins.
Nolte
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Department of Biophysics, Housman Medical Research Center, Boston University School of Medicine, Massachusetts 02118.
Atkinson
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D000595:Amino Acid Sequence; D016632:Apolipoprotein A-I / Q000737:chemistry*; D053318:Apolipoprotein E3; D001057:Apolipoproteins E / Q000097:blood / Q000737:chemistry*; D055592:Biophysical Phenomena; D001703:Biophysics; D002942:Circular Dichroism; D016384:Consensus Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D016632:Apolipoprotein A-I; D053318:Apolipoprotein E3; D001057:Apolipoproteins E