Structural and functional features of Drosophila chorion proteins s36 and s38 from analysis of primary structure and infrared spectroscopy.
Amino acid composition, Fourier transform analysis and secondary structure prediction methods strongly support a tripartite structure for Drosophila chorion proteins s36 and s38. Each protein consists of a central domain and two flanking 'arms'. The central domain contains tandemly repetitive peptides, which apparently generate a secondary structure of beta-sheet strands alternating with beta-turns, most probably, forming a twisted beta-pleated sheet or beta-barrel. The central domains of s36 and s38 share similarities, but they are recognizably different. The flanking 'arms', with different primary and secondary structure features, presumably serve protein-specific functions. The possible roles of the protein domains for the establishment of higher order structure in Drosophila chorion and the possible function of the molecules are discussed. The predicted secondary structure of Drosophila chorion proteins s36 and s38 is supported by experimental information obtained from Fourier transform infrared spectroscopic studies of Drosophila chorions.
Hamodrakas
S J
SJ
Department of Biochemistry, Cell and Molecular Biology and Genetics, University of Athens, Greece.
Batrinou
A
A
Christophoratou
T
T
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002823:Chorion / Q000737:chemistry; D004330:Drosophila / Q000032:analysis*; D004527:Egg Proteins / Q000032:analysis / Q000737:chemistry*; D005583:Fourier Analysis; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D013055:Spectrophotometry, Infrared
D000596:Amino Acids; D004527:Egg Proteins; C015753:chorion proteins