PMID: 2489096Oct 1, 1989Paper

Structural and functional features of Drosophila chorion proteins s36 and s38 from analysis of primary structure and infrared spectroscopy

International Journal of Biological Macromolecules
S J HamodrakasT Christophoratou

Abstract

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.

References

Jan 1, 1989·Molecular and Biochemical Parasitology·V RodriguesA J Simpson
Jan 1, 1984·Biology of the Cell·L H MargaritisK R Leonard
Jun 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·W OrrF C Kafatos
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Oct 27, 2009·Pathophysiology : the Official Journal of the International Society for Pathophysiology·Adamantia F FragopoulouLukas H Margaritis

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Citations

Oct 1, 1991·International Journal of Biological Macromolecules·A AggeliM Konsolaki

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