Abstract
The central domain is an evolutionarily conservative region that is invariant in length in the A and Hc-A families of silkmoth chorion proteins. This domain shows strong sixfold periodicities for various amino acid residues, such as glycine and large non-polar residues. The periodicities and their phase relationships, together with the documented prevalence of β-sheets and β-turns in the chorion, strongly support a secondary structure model in which short (4-residue) β-sheet strands alternate with β-turns, forming a compact antiparallel, probably twisted β-sheet. This structure should be important for the establishment of higher order structure in the chorion.
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