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. 1986 Jun 15;236(3):713–720. doi: 10.1042/bj2360713

Primary structure of a structural protein from the cuticle of the migratory locust, Locusta migratoria.

P Højrup, S O Andersen, P Roepstorff
PMCID: PMC1146903  PMID: 3790088

Abstract

The complete amino acid sequence of a structural protein isolated from pharate cuticle of the locust Locusta migratoria was determined. The protein has an unusual amino acid composition: 42% of the residues are alanine and only 14 of the 20 common amino acid residues are present. The primary structure consists of regions enriched in particular amino acid residues. The N-terminal region and a region close to the C-terminus are enriched in glycine. The rest of the protein is dominated by alanine, except for two short regions enriched in hydrophilic residues. Almost all the proline residues are situated in the alanine-rich regions in a conserved sequence 'A-A-P-A/V'. An internal duplication has taken place covering most of the protein except for the glycine-rich regions. Owing to the unusual features of the protein a combination of automated Edman degradations and plasma-desorption m.s. was used to determine the complete sequence. The protein does not show sequence homology to other proteins, but proteins divided into regions enriched in the same kind of amino acid residues have been isolated from other insect structures.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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