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Amino acid periodicities and their structural implications for the evolutionarily conservative central domain of some silkmoth chorion proteins.

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 beta-sheets and beta-turns in the chorion, strongly support a secondary structure model in which short (4-residue) beta-sheet strands alternate with beta-turns, forming a compact antiparallel, probably twisted beta-sheet. This structure should be important for the establishment of higher order structure in the chorion.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Hamodrakas SJ,Etmektzoglou T,Kafatos FC

doi

10.1016/0022-2836(85)90132-9

subject

Has Abstract

pub_date

1985-12-05 00:00:00

pages

583-9

issue

3

eissn

0022-2836

issn

1089-8638

pii

0022-2836(85)90132-9

journal_volume

186

pub_type

杂志文章

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