Molecular architecture of helicoidal proteinaceous eggshells.
I will not attempt to summarize this chapter, which is already a summary. I merely wish to point out that experimental and theoretical evidence to date clearly suggests that antiparallel beta-pleated sheet dictates self-assembly in helicoidal proteinaceous eggshells. Molecular details of this process have started to become clear after the development of the specific, most probably correct, protein structural models in the case of the silkmoths, where amino acid information is available and with the help of several experimental techniques. However, for people seeking universal mechanisms the picture should still be far from complete. Several analogous systems should be studied before providing final answers.
Hamodrakas
S J
SJ
Department of Biochemistry, Cell and Molecular Biology, and Genetics, University of Athens, Panepistimiopolis, Greece.
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx; D004527:Egg Proteins / Q000737:chemistry*; D004528:Egg Shell / Q000737:chemistry* / Q000648:ultrastructure; D005399:Fishes; D008969:Molecular Sequence Data; D009024:Morphogenesis; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
D004527:Egg Proteins